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Conserved domains on  [gi|114594366|ref|XP_001160004|]
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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 2.80e-44

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


:

Pssm-ID: 397055  Cd Length: 129  Bit Score: 153.96  E-value: 2.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  103 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 176
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 114594366  177 SEYMKALINKKELLSEFYEPNALMMEEEGA-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 ...
562-608 5.54e-20

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: 83.62  E-value: 5.54e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 114594366 562 CQLCQEDG---SLTKNVCKNCSGTFCDACSTNELPLPSSI-KLERVCNPCH 608
Cdd:cd15744    2 CSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
Smc super family cl34174
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
256-496 1.81e-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: 60.88  E-value: 1.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  256 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKGPKQDR 335
Cdd:COG1196   710 QLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALA-KLKEEIEELEEKR 788
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  336 TAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS 415
Cdd:COG1196   789 QALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEEL 868
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  416 DlgvKQKSELNSRLEEKTNQmaatIKQLEQRLRQAERSRQSAELDNrlfkQDFGDKINSLQLEVEELTRQRNQLELELKQ 495
Cdd:COG1196   869 E---AEKEELEDELKELEEE----KEELEEELRELESELAELKEEI----EKLRERLEELEAKLERLEVELPELEEELEE 937

                  .
gi 114594366  496 E 496
Cdd:COG1196   938 E 938
 
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 2.80e-44

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


Pssm-ID: 397055  Cd Length: 129  Bit Score: 153.96  E-value: 2.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  103 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 176
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 114594366  177 SEYMKALINKKELLSEFYEPNALMMEEEGA-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 ...
562-608 5.54e-20

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: 83.62  E-value: 5.54e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 114594366 562 CQLCQEDG---SLTKNVCKNCSGTFCDACSTNELPLPSSI-KLERVCNPCH 608
Cdd:cd15744    2 CSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
RUN smart00593
domain involved in Ras-like GTPase signaling;
163-225 6.37e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736  Cd Length: 64  Bit Score: 78.04  E-value: 6.37e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114594366   163 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-EEEGAIIAGLLVGLNVIDANFCMK 225
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
256-496 1.81e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 60.88  E-value: 1.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  256 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKGPKQDR 335
Cdd:COG1196   710 QLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALA-KLKEEIEELEEKR 788
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  336 TAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS 415
Cdd:COG1196   789 QALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEEL 868
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  416 DlgvKQKSELNSRLEEKTNQmaatIKQLEQRLRQAERSRQSAELDNrlfkQDFGDKINSLQLEVEELTRQRNQLELELKQ 495
Cdd:COG1196   869 E---AEKEELEDELKELEEE----KEELEEELRELESELAELKEEI----EKLRERLEELEAKLERLEVELPELEEELEE 937

                  .
gi 114594366  496 E 496
Cdd:COG1196   938 E 938
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
254-531 2.70e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.46  E-value: 2.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   254 DGQITAILDQKNYVEELNRHLN---ATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKG 330
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA-RLEAEVEQ 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   331 PKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 410
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   411 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRqsAELDNRLfkQDFGDKINSLQLEVEELTRQRNQLE 490
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESEL--EALLNERASLEEALALLRSELEELS 900
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 114594366   491 LELKQEKERRLQNDRSIPGRGSQKSESKMD-GKHKMQEENVK 531
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRlEGLEVRIDNLQ 942
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
556-611 3.35e-08

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: 50.51  E-value: 3.35e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   556 SEKPQVCQLCQEDGSLT--KNVCKNCSGTFCDACSTNELPLPSS--IKLERVCNPCHKHL 611
Cdd:smart00064   7 DEEVSNCMGCGKEFNLTkrRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENL 66
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
561-613 6.43e-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: 49.69  E-value: 6.43e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 114594366  561 VCQLCQEDGSLT--KNVCKNCSGTFCDACSTNELPLPSSI---KLERVCNPCHKHLMK 613
Cdd:pfam01363  11 VCMICSKPFTFFrrRHHCRNCGRVFCSACSSKKASLLPELgsnKPVRVCDACYDTLQK 68
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
310-543 3.85e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 50.12  E-value: 3.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  310 QEEMERVKEESSYILESNRKgPKQDRTAEGQALSEARKHLKEETQLRLDVEKELE--MQISMRQEME------LAMKM-- 379
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRK-LEEAEKARQAEMDRQAAIYAEQERMAMERERELEriRQEERKRELErirqeeIAMEIsr 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  380 ---LEKDVCEKQDALVSLRQQLDDLRALK-----HELAFKLQSSDLGVKQKSELNSR------LEEKTNQMAATIKQLEQ 445
Cdd:pfam17380 377 mreLERLQMERQQKNERVRQELEAARKVKileeeRQRKIQQQKVEMEQIRAEQEEARqrevrrLEEERAREMERVRLEEQ 456
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  446 -RLRQAERSRQSAELDNRlfKQDFGDKINSLQLEVEELTRQRNQLELELKQEKERRLQNDRSIPGRGSQKSESKM--DGK 522
Cdd:pfam17380 457 eRQQQVERLRQQEEERKR--KKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEER 534
                         250       260
                  ....*....|....*....|.
gi 114594366  523 HKMQEENVKLKKPLEESHRLQ 543
Cdd:pfam17380 535 RREAEEERRKQQEMEERRRIQ 555
PRK11281 PRK11281
mechanosensitive channel MscK;
267-489 6.71e-06

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 49.14  E-value: 6.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  267 VEELNRHLNATVNNLQakvdaleksntKLTEELAVANNRIITLQEEMERVKEESSY----------ILESNRKGPKQDR- 335
Cdd:PRK11281  123 LRQLESRLAQTLDQLQ-----------NAQNDLAEYNSQLVSLQTQPERAQAALYAnsqrlqqirnLLKGGKVGGKALRp 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  336 ------TAEgQALSEA-----RKHLKEETQL------RLDVEKE----LEMQISMRQEM--ELAMKMLEKDVCEKQDALV 392
Cdd:PRK11281  192 sqrvllQAE-QALLNAqndlqRKSLEGNTQLqdllqkQRDYLTAriqrLEHQLQLLQEAinSKRLTLSEKTVQEAQSQDE 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  393 SLRQQLDDLraLKHELAFKLQSSDLGVKQKSELNSRLEEktNQMaatIKQLEQRLRQAERS--------RQSAELDNRLF 464
Cdd:PRK11281  271 AARIQANPL--VAQELEINLQLSQRLLKATEKLNTLTQQ--NLR---VKNWLDRLTQSERNikeqisvlKGSLLLSRILY 343
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 114594366  465 KQ-----------DFGDKINSLQLEVEELTRQRNQL 489
Cdd:PRK11281  344 QQqqalpsadlieGLADRIADLRLEQFEINQQRDAL 379
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
259-550 2.45e-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: 44.13  E-value: 2.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 259 AILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyilESNRKGPkqdrtae 338
Cdd:NF033930 105 AYVKYRKAQRRKKSDYKKKLAEADKKIDEAKKKQKEAKAEFNKVRAKVVPEAEELAETKKKAE---EAKAEEP------- 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 339 gqalsEARKHLKEETQLRLDVEKELEmqismRQEMELAMKMLEKDVCEKQDAlvSLRQQLDDLralKHELAfKLQSSDLG 418
Cdd:NF033930 175 -----VAKKKVDEAKKKVEEAKKKVE-----AEEAEIEKLQNEEVALEAKIA--ELENQVDNL---EKELA-EIDESDSE 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 419 --VKQ--KSELNSRLEEKTNQMAATIKQLEQRLRQAE-RSRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRNQLELEL 493
Cdd:NF033930 239 dyIKEglRAPLESELDAKQAKLAKKQTELEKLLDSLDpEGKTQDELDKEAAEEELSKKIDELDNEVAKLEKEVSDLENSD 318
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114594366 494 ----KQEKErRLQNDRSIPGRGSQKSESKMDgkhKMQEEnvkLKKPLEESHRLQPHPMDEQ 550
Cdd:NF033930 319 nnvaDYYKE-ALEKDLATKKAELEKTQKDLD---KALNE---LGPDGDEEETPAPAPQPEQ 372
M_group_A_cterm NF033777
M protein C-terminal domain; M protein (emm) is an important virulence protein and ...
267-409 1.78e-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: 40.20  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 267 VEELNRHLNATVNNLQAKVDALEKSNTKLTEELAvannriiTLQEEMERVKEESSyILESNRKGPKQDRTAEGQALSEAR 346
Cdd:NF033777   7 LEEQNKISEASRKGLRRDLDASREAKKQVEKDLA-------NLTAELDKVKEEKQ-ISDASRQGLRRDLDASREAKKQVE 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114594366 347 KHLKEETQLRLDVEKelemqisMRQEMELAMKMLEKDVCEKQDALVSlrqqldDLRALKHELA 409
Cdd:NF033777  79 KALEEANSKLAALEK-------LNKELEESKKLTEKEKAELQAKLEA------EAKALKEQLA 128
 
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 2.80e-44

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


Pssm-ID: 397055  Cd Length: 129  Bit Score: 153.96  E-value: 2.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  103 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 176
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 114594366  177 SEYMKALINKKELLSEFYEPNALMMEEEGA-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 ...
562-608 5.54e-20

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: 83.62  E-value: 5.54e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 114594366 562 CQLCQEDG---SLTKNVCKNCSGTFCDACSTNELPLPSSI-KLERVCNPCH 608
Cdd:cd15744    2 CSLCQEDFaslALPKHNCYNCGGTFCDACSSNELPLPSSIyEPARVCDVCY 52
RUN smart00593
domain involved in Ras-like GTPase signaling;
163-225 6.37e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736  Cd Length: 64  Bit Score: 78.04  E-value: 6.37e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114594366   163 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEPNALMM-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; ...
562-608 1.62e-14

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: 68.18  E-value: 1.62e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 114594366 562 CQLCQEDGSLT--KNVCKNCSGTFCDACSTNELPLPSSIKLERVCNPCH 608
Cdd:cd15721   10 CQQCEKEFSLSrrKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
562-618 5.79e-12

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: 61.19  E-value: 5.79e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 114594366 562 CQLCQEDGSLT--KNVCKNCSGTFCDACSTNELPLPSSIKLERVCNPCHKHLMKQYSTS 618
Cdd:cd15759   13 CKLCEKEFSLSkrKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSCHAMLIQRCSSN 71
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
562-616 1.42e-11

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: 60.08  E-value: 1.42e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 114594366 562 CQLCQEDGSLT--KNVCKNCSGTFCDACSTNELPLPSSIKLERVCNPCHKHLMKQYS 616
Cdd:cd15758   15 CKQCEKEFSISrrKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCS 71
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
256-496 1.81e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 60.88  E-value: 1.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  256 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKGPKQDR 335
Cdd:COG1196   710 QLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALA-KLKEEIEELEEKR 788
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  336 TAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS 415
Cdd:COG1196   789 QALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEEL 868
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  416 DlgvKQKSELNSRLEEKTNQmaatIKQLEQRLRQAERSRQSAELDNrlfkQDFGDKINSLQLEVEELTRQRNQLELELKQ 495
Cdd:COG1196   869 E---AEKEELEDELKELEEE----KEELEEELRELESELAELKEEI----EKLRERLEELEAKLERLEVELPELEEELEE 937

                  .
gi 114594366  496 E 496
Cdd:COG1196   938 E 938
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
272-540 2.05e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 60.88  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  272 RHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTAEGQA--LSEARKHL 349
Cdd:COG1196   235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIslLRERLEEL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  350 KEETQLRLDVEKELEMQISMRQEMELAMKMLEKdvcEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-SELNSR 428
Cdd:COG1196   315 ENELEELEERLEELKEKIEALKEELEERETLLE---ELEQLLAELEEAKEELEEKLSALLEELEELFEALREElAELEAE 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  429 LEEKTNQMAATIKQLEQ-RLRQAERSRQSAELDNRLFK------------QDFGDKINSLQLEVEELTRQRNQLELEL-- 493
Cdd:COG1196   392 LAEIRNELEELKREIESlEERLERLSERLEDLKEELKEleaeleelqtelEELNEELEELEEQLEELRDRLKELERELae 471
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 114594366  494 KQEKERRLQNDRSIPGRGSQKSESKMDGKHKMQEENVKLKKPLEESH 540
Cdd:COG1196   472 LQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVY 518
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
254-531 2.70e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.46  E-value: 2.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   254 DGQITAILDQKNYVEELNRHLN---ATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKG 330
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA-RLEAEVEQ 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   331 PKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 410
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   411 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRqsAELDNRLfkQDFGDKINSLQLEVEELTRQRNQLE 490
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI--EELESEL--EALLNERASLEEALALLRSELEELS 900
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 114594366   491 LELKQEKERRLQNDRSIPGRGSQKSESKMD-GKHKMQEENVK 531
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRlEGLEVRIDNLQ 942
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
562-608 9.90e-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: 51.38  E-value: 9.90e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 114594366 562 CQLCQEDGSLT--KNVCKNCSGTFCDACSTNELPLPS--SIKLERVCNPCH 608
Cdd:cd00065    2 CMLCGKKFSLFrrRHHCRRCGRVFCSKCSSKKLPLPSfgSGKPVRVCDSCY 52
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
268-541 1.37e-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: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  268 EELNRHLNATVNNL---QAKVDALEKSNTKLTEELAVANnRIITLQEEMERvKEESSYILESNRKGPKQDRTAEgqALSE 344
Cdd:COG1196   175 EEAERKLERTEENLerlEDLLEELEKQLEKLERQAEKAE-RYQELKAELRE-LELALLLAKLKELRKELEELEE--ELSR 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  345 ARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK-- 422
Cdd:COG1196   251 LEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELke 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  423 --SELNSRLEEKTNQM---AATIKQLEQRLRQAE--RSRQSAELDNRlfKQDFGDKINSLQLEVEELTRQRNQLELELKQ 495
Cdd:COG1196   331 kiEALKEELEERETLLeelEQLLAELEEAKEELEekLSALLEELEEL--FEALREELAELEAELAEIRNELEELKREIES 408
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 114594366  496 EKERRLQNDRSIPGRGSQKS--ESKMDGKHKMQEENVKLKKPLEESHR 541
Cdd:COG1196   409 LEERLERLSERLEDLKEELKelEAELEELQTELEELNEELEELEEQLE 456
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
556-611 3.35e-08

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: 50.51  E-value: 3.35e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   556 SEKPQVCQLCQEDGSLT--KNVCKNCSGTFCDACSTNELPLPSS--IKLERVCNPCHKHL 611
Cdd:smart00064   7 DEEVSNCMGCGKEFNLTkrRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENL 66
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
256-502 5.26e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 56.26  E-value: 5.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  256 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilesnRKGPKQDR 335
Cdd:COG1196   717 QLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEE--------IEELEEKR 788
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  336 TAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS 415
Cdd:COG1196   789 QALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEEL 868
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  416 DLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRLFKQdfgdKINSLQLEVEELTRQ-RNQLELELK 494
Cdd:COG1196   869 EAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEA----KLERLEVELPELEEElEEEYEDTLE 944

                  ....*...
gi 114594366  495 QEKERRLQ 502
Cdd:COG1196   945 TELEREIE 952
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
561-613 6.43e-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: 49.69  E-value: 6.43e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 114594366  561 VCQLCQEDGSLT--KNVCKNCSGTFCDACSTNELPLPSSI---KLERVCNPCHKHLMK 613
Cdd:pfam01363  11 VCMICSKPFTFFrrRHHCRNCGRVFCSACSSKKASLLPELgsnKPVRVCDACYDTLQK 68
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
251-500 1.28e-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: 1.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   251 TEGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilesnRKG 330
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--------LES 828
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   331 PKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 410
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   411 KLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLrqaeRSRQSAELDNRL-FKQDFGDKINSLQLEVEELTRQRNQL 489
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL----SEEYSLTLEEAEaLENKIEDDEEEARRRLKRLENKIKEL 984
                          250
                   ....*....|....*...
gi 114594366   490 -------ELELKQEKERR 500
Cdd:TIGR02168  985 gpvnlaaIEEYEELKERY 1002
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
309-567 2.44e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.92  E-value: 2.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   309 LQEEMERVKEESsYILESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQ 388
Cdd:TIGR02169  672 EPAELQRLRERL-EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   389 DALVSLRQQLDDLRALKHEL-----AFKLQSSDLG-----------VKQKSELN---SRLEEKTNQMAATIKQLEQRLRQ 449
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELeedlhKLEEALNDLEarlshsripeiQAELSKLEeevSRIEARLREIEQKLNRLTLEKEY 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   450 AERSRQSAELDNRLFK---QDFGDKINSLQLEVEELTRQRNQLELELKQ--------EKER-RLQNDRSIPGRGSQKSES 517
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEELEELEAALRDlesrlgdlKKERdELEAQLRELERKIEELEA 910
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 114594366   518 KMD-GKHKMQEENVKLKKPLEE-SHRLQPHPMDEQDQLLLSEKPQVCQLCQE 567
Cdd:TIGR02169  911 QIEkKRKRLSELKAKLEALEEElSEIEDPKGEDEEIPEEELSLEDVQAELQR 962
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
561-608 2.59e-07

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: 47.91  E-value: 2.59e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 114594366 561 VCQLCQEDGSLT--KNVCKNCSGTFCDACSTNELPLP--SSIKLERVCNPCH 608
Cdd:cd15735    8 VCMRCRTAFTFTnrKHHCRNCGGVFCQQCSSKSLPLPhfGINQPVRVCDGCY 59
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
264-490 3.30e-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: 53.52  E-value: 3.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   264 KNYVEELNRhLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGpKQDRTAEGQALS 343
Cdd:TIGR02168  263 QELEEKLEE-LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL-ESKLDELAEELA 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   344 EARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRA-----------LKHELAFKL 412
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeierlearlerLEDRRERLQ 420
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   413 Q-----SSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRLFkQDFGDKINSLQLEVEELTRQRN 487
Cdd:TIGR02168  421 QeieelLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLERLQE 499

                   ...
gi 114594366   488 QLE 490
Cdd:TIGR02168  500 NLE 502
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
251-501 5.25e-07

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 52.79  E-value: 5.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  251 TEGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEE-SSYILESNRK 329
Cdd:COG1196   747 EELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERElESLEQRRERL 826
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  330 GPK----QDRTAEGQA-LSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMK-------MLEKDVCEKQDALVSLRQQ 397
Cdd:COG1196   827 EQEieelEEEIEELEEkLDELEEELEELEKELEELKEELEELEAEKEELEDELKeleeekeELEEELRELESELAELKEE 906
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  398 LDDLRALKHELAFKLQssdlgvKQKSELNSRLEEKTNQMAATI-KQLEQRLRQAERSRQSAELDNRLFKQDFG---DKIN 473
Cdd:COG1196   907 IEKLRERLEELEAKLE------RLEVELPELEEELEEEYEDTLeTELEREIERLEEEIEALGPVNLRAIEEYEeveERYE 980
                         250       260       270
                  ....*....|....*....|....*....|.
gi 114594366  474 SLQLEVEELTRQRNQLEL---ELKQEKERRL 501
Cdd:COG1196   981 ELKSQREDLEEAKEKLLEvieELDKEKRERF 1011
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
562-611 1.13e-06

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: 45.85  E-value: 1.13e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 114594366 562 CQLCQEDGSLT--KNVCKNCSGTFCDACSTNELPLPSSIKLERVCNPCHKHL 611
Cdd:cd15730   12 CMACGKGFSVTvrKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDACFDDL 63
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
562-607 2.09e-06

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: 45.02  E-value: 2.09e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 114594366 562 CQLCQEDGS--LTKNVCKNCSGTFCDACSTNELPLPSS--IKLERVCNPC 607
Cdd:cd15734   11 CSVCKRPFSprLSKHHCRACGQGVCDDCSKNRRPVPSRgwDHPVRVCDPC 60
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
562-607 2.30e-06

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: 45.28  E-value: 2.30e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 114594366 562 CQLCQED--GSLTKNVCKNCSGTFCDACSTNELPLPSSIKLE--RVCNPC 607
Cdd:cd15732   11 CYGCEREfwLASRKHHCRNCGNVFCGSCCNQKLPVPSQQLFEpsRVCKSC 60
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
254-502 2.86e-06

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


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 50.53  E-value: 2.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 254 DGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERvKEESSYILESNRKGPKQ 333
Cdd:COG0419  318 EELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEK-ALERLKQLEEAIQELKE 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 334 DRTAEGQALSEARKHLKEETQLRLDVEKELE---MQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAF 410
Cdd:COG0419  397 ELAELSAALEEIQEELEELEKELEELERELEeleEEIKKLEEQINQLESKELMIAELAGAGEKCPVCGQELPEEHEKELL 476
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 411 KLQSSDLGVKQKSELNSRLEEKTNQmaaTIKQLEQRLRQAERSRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRNQLE 490
Cdd:COG0419  477 ELYELELEELEEELSREKEEAELRE---EIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKLQ 553
                        250
                 ....*....|..
gi 114594366 491 LELKQEKERRLQ 502
Cdd:COG0419  554 LQQLKEELRQLE 565
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
310-543 3.85e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 50.12  E-value: 3.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  310 QEEMERVKEESSYILESNRKgPKQDRTAEGQALSEARKHLKEETQLRLDVEKELE--MQISMRQEME------LAMKM-- 379
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRK-LEEAEKARQAEMDRQAAIYAEQERMAMERERELEriRQEERKRELErirqeeIAMEIsr 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  380 ---LEKDVCEKQDALVSLRQQLDDLRALK-----HELAFKLQSSDLGVKQKSELNSR------LEEKTNQMAATIKQLEQ 445
Cdd:pfam17380 377 mreLERLQMERQQKNERVRQELEAARKVKileeeRQRKIQQQKVEMEQIRAEQEEARqrevrrLEEERAREMERVRLEEQ 456
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  446 -RLRQAERSRQSAELDNRlfKQDFGDKINSLQLEVEELTRQRNQLELELKQEKERRLQNDRSIPGRGSQKSESKM--DGK 522
Cdd:pfam17380 457 eRQQQVERLRQQEEERKR--KKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEER 534
                         250       260
                  ....*....|....*....|.
gi 114594366  523 HKMQEENVKLKKPLEESHRLQ 543
Cdd:pfam17380 535 RREAEEERRKQQEMEERRRIQ 555
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
561-611 4.92e-06

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: 44.30  E-value: 4.92e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 114594366 561 VCQLCQEDGSLT--KNVCKNCSGTFCDACSTNELPLPS-SIKLE-RVCNPCHKHL 611
Cdd:cd15720    7 ECHRCRVQFGVFqrKHHCRACGQVFCGKCSSKSSTIPKfGIEKEvRVCDPCYEKL 61
PRK11281 PRK11281
mechanosensitive channel MscK;
267-489 6.71e-06

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 49.14  E-value: 6.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  267 VEELNRHLNATVNNLQakvdaleksntKLTEELAVANNRIITLQEEMERVKEESSY----------ILESNRKGPKQDR- 335
Cdd:PRK11281  123 LRQLESRLAQTLDQLQ-----------NAQNDLAEYNSQLVSLQTQPERAQAALYAnsqrlqqirnLLKGGKVGGKALRp 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  336 ------TAEgQALSEA-----RKHLKEETQL------RLDVEKE----LEMQISMRQEM--ELAMKMLEKDVCEKQDALV 392
Cdd:PRK11281  192 sqrvllQAE-QALLNAqndlqRKSLEGNTQLqdllqkQRDYLTAriqrLEHQLQLLQEAinSKRLTLSEKTVQEAQSQDE 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  393 SLRQQLDDLraLKHELAFKLQSSDLGVKQKSELNSRLEEktNQMaatIKQLEQRLRQAERS--------RQSAELDNRLF 464
Cdd:PRK11281  271 AARIQANPL--VAQELEINLQLSQRLLKATEKLNTLTQQ--NLR---VKNWLDRLTQSERNikeqisvlKGSLLLSRILY 343
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 114594366  465 KQ-----------DFGDKINSLQLEVEELTRQRNQL 489
Cdd:PRK11281  344 QQqqalpsadlieGLADRIADLRLEQFEINQQRDAL 379
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
242-500 6.90e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.97  E-value: 6.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  242 LKDGNSSKGTEGDGQITAILDQKNYVEELNRHLNATvnNLQAKVDALEKSNTkltEELAVANNRIITL-------QEEME 314
Cdd:pfam17380 318 LEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELERIRQ---EEIAMEISRMRELerlqmerQQKNE 392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  315 RVKEE-----SSYILESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKM--LEKDVCEK 387
Cdd:pfam17380 393 RVRQEleaarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVerLRQQEEER 472
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  388 QDALVSLRQQLDDlRALKHELAFKLQSSDLGVKQKS---ELNSR--LEEKTNQMAATIKQLEQRLRQAERSRQSAELDNR 462
Cdd:pfam17380 473 KRKKLELEKEKRD-RKRAEEQRRKILEKELEERKQAmieEERKRklLEKEMEERQKAIYEEERRREAEEERRKQQEMEER 551
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 114594366  463 LFKQDFGDKINSLQLEVEELTRQRNQLELELKQEKERR 500
Cdd:pfam17380 552 RRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
252-514 8.55e-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: 8.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   252 EGDGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEElavannRIITLQEEMERVKEESSYILESNRKGP 331
Cdd:TIGR02169  241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEKE 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   332 KQDRTAEGQA----------LSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLE---KDVCEKQDALVSLRQQL 398
Cdd:TIGR02169  315 RELEDAEERLakleaeidklLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdKEFAETRDELKDYREKL 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   399 DDLralKHELAFKLQSSDLGVKQKSELNSRL----------EEKTNQMAATIKQLEQRLRQAERSRQSAELDnrlfKQDF 468
Cdd:TIGR02169  395 EKL---KREINELKRELDRLQEELQRLSEELadlnaaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAAD----LSKY 467
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 114594366   469 GDKINSLQLEVEELTRQRNQLELELKQ-EKERRLQNDRSIPGRGSQK 514
Cdd:TIGR02169  468 EQELYDLKEEYDRVEKELSKLQRELAEaEAQARASEERVRGGRAVEE 514
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
277-538 1.67e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 277 TVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTAEgqalSEARKHLKEETQLR 356
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT----EEHRKELLEEYTAE 460
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 357 L-DVEKELEMQISMRQEMELAMKMLEKdVCEKQDALVSLRQQLDDLRALKHELAfKLQSSDLgvKQKSELNSRLEEKTNQ 435
Cdd:PRK03918 461 LkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLK-KYNLEEL--EKKAEEYEKLKEKLIK 536
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 436 MAATIKQLEQRLRQAErsrqsaELDNRLFKQDfgDKINSLQLEVEELTRQRNQLELELKQEKERRLQNDRSIpgrgSQKS 515
Cdd:PRK03918 537 LKGEIKSLKKELEKLE------ELKKKLAELE--KKLDELEEELAELLKELEELGFESVEELEERLKELEPF----YNEY 604
                        250       260
                 ....*....|....*....|...
gi 114594366 516 ESKMDGKHKMQEENVKLKKPLEE 538
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEE 627
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
256-458 2.47e-05

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


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 46.94  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 256 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESsyilesnrkgpkQDR 335
Cdd:COG4372   82 QLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQA------------QDL 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 336 TAEGQALSEARKHLKEETQLRLDVEKELEMQISM----RQEMELAMKMLE---KDVCEKQDALVSLRQQLDDLRALKHEL 408
Cdd:COG4372  150 QTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQlksqVLDLKLRSAQIEqeaQNLATRANAAQARTEELARRAAAAQQT 229
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 114594366 409 AFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAE 458
Cdd:COG4372  230 AQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLE 279
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
264-452 2.54e-05

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


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 46.94  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 264 KNYVEElNRHLNATVNNLQAKVDALEKSNTKLteelavaNNRIITLQEEMERVKEESSYIleSNRKGPKQDRTAEGQALS 343
Cdd:COG4372  154 KTLAEQ-RRQLEAQAQSLQASQKQLQASATQL-------KSQVLDLKLRSAQIEQEAQNL--ATRANAAQARTEELARRA 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 344 EARKHLKEETQLRLDVEKELEMQISMRQEmelamkmlekDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS-DLGVKQK 422
Cdd:COG4372  224 AAAQQTAQAIQQRDAQISQKAQQIAARAE----------QIRERERQLQRLETAQARLEQEVAQLEAYYQAYvRLRQQAA 293
                        170       180       190
                 ....*....|....*....|....*....|....
gi 114594366 423 SELNSRLE----EKTNQMAATIKQLEQRLRQAER 452
Cdd:COG4372  294 ATQRGQVLagaaQRVAQAQAQAQAQAQLLSSANR 327
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
252-507 3.31e-05

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


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 47.06  E-value: 3.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 252 EGDGQITAILDQKnyvEELNRHLNATVNNLQAKVDALEKSN-TKLTEELAVANNRIITLQEEMERVKEESSYILESNRKG 330
Cdd:COG0419  189 ELEGQLSELLEDI---EDLLEALEEELKELKKLEEIQEEQEeEELEQEIEALEERLAELEEEKERLEELKARLLEIESLE 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 331 PKQDRTAEgqalSEARKHLKEETQLRLDVE--KELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHEL 408
Cdd:COG0419  266 LEALKIRE----EELRELERLLEELEEKIErlEELEREIEELEEELEGLRALLEELEELLEKLKSLEERLEKLEEKLEKL 341
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 409 AFKLQS-SDLGVKQKSELNSRLEEKTNQMAATIKQLEQRL-RQAERSRQSAELDNRLfkQDFGDKINSLQLEVEELTRQR 486
Cdd:COG0419  342 ESELEElAEEKNELAKLLEERLKELEERLEELEKELEKALeRLKQLEEAIQELKEEL--AELSAALEEIQEELEELEKEL 419
                        250       260
                 ....*....|....*....|.
gi 114594366 487 NQLELELKQEKERRLQNDRSI 507
Cdd:COG0419  420 EELERELEELEEEIKKLEEQI 440
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
562-607 4.07e-05

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: 41.33  E-value: 4.07e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 114594366 562 CQLCQEDGSLT--KNVCKNCSGTFCDACSTNELPL--PSSIKLERVCNPC 607
Cdd:cd15745    2 CAICAKAFSLFrrKYVCRLCGGVVCHSCSSEDLVLsvPDTCIYLRVCKTC 51
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
576-607 6.86e-05

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: 41.18  E-value: 6.86e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 114594366 576 CKNCSGTFCDACSTNELPLPSSI--KLERVCNPC 607
Cdd:cd15731   30 CRNCGKIFCSRCSSNSVPLPRYGqmKPVRVCNHC 63
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
551-611 8.95e-05

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: 40.83  E-value: 8.95e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114594366 551 DQLLLSEKPQVCQLCQEDGSLT--KNVCKNCSGTFCDACSTNELPLPS--SIKLERVCNPCHKHL 611
Cdd:cd15719    1 DHWVKDEGGDSCTGCSVRFSLTerRHHCRNCGQLFCSKCSRFESEIRRlrISRPVRVCQACYNIL 65
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
557-607 9.21e-05

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: 40.82  E-value: 9.21e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 114594366 557 EKPQVCQLCQEDGSLT--KNVCKNCSGTFCDACSTNELPLP--SSIKLERVCNPC 607
Cdd:cd15727    8 KECPVCMSCKKKFDFFkrRHHCRRCGKCFCSDCCSNKVPLPrmCFVDPVRVCNEC 62
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
350-538 9.59e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 9.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   350 KEETQLRL-----------DVEKELEMQI-SMRQEMELAMKMLEKDVCEKQdalVSLRQQLDDLRALKHELAFKLQssdl 417
Cdd:TIGR02168  174 RKETERKLertrenldrleDILNELERQLkSLERQAEKAERYKELKAELRE---LELALLVLRLEELREELEELQE---- 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   418 gvkQKSELNSRLEEKTNQMAATIKQLEQ-RLRQAERSRQSAELDNRLFkqdfgdkinSLQLEVEELTRQrnqleLELKQE 496
Cdd:TIGR02168  247 ---ELKEAEEELEELTAELQELEEKLEElRLEVSELEEEIEELQKELY---------ALANEISRLEQQ-----KQILRE 309
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 114594366   497 KERRLQNDRSIPGRGSQKSESKMDgkhKMQEENVKLKKPLEE 538
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLD---ELAEELAELEEKLEE 348
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
561-608 1.10e-04

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: 40.36  E-value: 1.10e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 114594366 561 VCQLCQEDGSLTK--NVCKNCSGTFCDACSTNELPLPSSI---KLERVCNPCH 608
Cdd:cd15760    7 RCDVCRKKFGLFKrrHHCRNCGDSFCSEHSSRRIPLPHLGplgVPQRVCDRCF 59
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
262-557 1.75e-04

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


Pssm-ID: 401982 [Multi-domain]  Cd Length: 765  Bit Score: 44.43  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  262 DQKNYVEELNRHLNAT---VNNLQAKVDAL-----EKSNT---------KLTEE--------------LAVANNRIITLQ 310
Cdd:pfam10174 320 DCKQHIEVLKESLTAKeqrAAILQTEVDALrlrleEKESFlnkktkqlqDLTEEkstlageirdlkdmLDVKERKINVLQ 399
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  311 EEMERVKE---ESSYILESNR---KGPKQDRTAEGQALSEARKHL--KEETQLRLDVEKELEMQI------SMRQEMELA 376
Cdd:pfam10174 400 KKIENLQEqlrDKDKQLAGLKervKSLQTDSSNTDTALTTLEEALseKERIIERLKEQREREDRErleeleSLKKENKDL 479
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  377 ---MKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEektnqmaatiKQLEQRLRQAERS 453
Cdd:pfam10174 480 kekVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAIEQKKEECSKLE----------NQLKKAHNAEEAV 549
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  454 RQSAELDNRL--FKQD---FGDKINSLQLEVEELTRQRNQLELElKQEKERRLQN-DRSIPGRGSQKSESKMDGKHKMQE 527
Cdd:pfam10174 550 RTNPEINDRIrlLEQEvarYKEESGKAQAEVERLLGILREVENE-KNDKDKKIAElESLTLRQMKEQNKKVANIKHKQQE 628
                         330       340       350
                  ....*....|....*....|....*....|
gi 114594366  528 ENVKLKKPLEESHRLQPHPMDEQDQLLLSE 557
Cdd:pfam10174 629 EKKKGAQLLEEARRREDNLADNSQHLQLEE 658
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
312-455 1.86e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.34  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  312 EMERVKEES---SYILESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQ 388
Cdd:pfam17380 447 EMERVRLEEqerQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQ 526
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114594366  389 DALV--SLRQQLDDLRALKHELAFKLQSSDlGVKQKSELNSRLE--EKTNQMAATIKQLEQRLRQAERSRQ 455
Cdd:pfam17380 527 KAIYeeERRREAEEERRKQQEMEERRRIQE-QMRKATEERSRLEamEREREMMRQIVESEKARAEYEATTP 596
mukB PRK04863
chromosome partition protein MukB;
342-508 2.29e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.56  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  342 LSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEK--DVCEKQDALVSLRQQLDDLRALKHeLAFKLQssdlGV 419
Cdd:PRK04863  444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiaGEVSRSEAWDVARELLRRLREQRH-LAEQLQ----QL 518
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  420 KQK-SELNSRLEEKtnqmaatiKQLEQRLRQAERsRQSAELDNRLFKQDF----GDKINSLQLEVEELTRQRNQLELELK 494
Cdd:PRK04863  519 RMRlSELEQRLRQQ--------QRAERLLAEFCK-RLGKNLDDEDELEQLqeelEARLESLSESVSEARERRMALRQQLE 589
                         170
                  ....*....|....
gi 114594366  495 QEKERRLQNDRSIP 508
Cdd:PRK04863  590 QLQARIQRLAARAP 603
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
260-492 2.31e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.29  E-value: 2.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   260 ILDQK--NYVEELnRHLNATVNNLQAKVDALEKSNTKLTEELAvaNNRIITLQEEMERVKEESSYILESNR--KGPKQDR 335
Cdd:TIGR02169  748 SLEQEieNVKSEL-KELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLReiEQKLNRL 824
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   336 TAEGQALSEARKHLKEETQLRLDVEKELEMQIsmrQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS 415
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI---ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 114594366   416 DLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAErsrqsaeldnRLFKQDFGDKINSLQLEVEELTRQRNQLELE 492
Cdd:TIGR02169  902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE----------DPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
258-431 2.35e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 44.32  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  258 TAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKGPKQDRTA 337
Cdd:COG1196   351 QLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLE-RLSERLEDLKEELKE 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  338 EGQALSEARKHLKEETQLRLDVEKELEMQISMRQEmelamkmLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDL 417
Cdd:COG1196   430 LEAELEELQTELEELNEELEELEEQLEELRDRLKE-------LERELAELQEELQRLEKELSSLEARLDRLEAEQRASQG 502
                         170
                  ....*....|....
gi 114594366  418 GVKQKSELNSRLEE 431
Cdd:COG1196   503 VRAVLEALESGLPG 516
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
259-550 2.45e-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: 44.13  E-value: 2.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 259 AILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSyilESNRKGPkqdrtae 338
Cdd:NF033930 105 AYVKYRKAQRRKKSDYKKKLAEADKKIDEAKKKQKEAKAEFNKVRAKVVPEAEELAETKKKAE---EAKAEEP------- 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 339 gqalsEARKHLKEETQLRLDVEKELEmqismRQEMELAMKMLEKDVCEKQDAlvSLRQQLDDLralKHELAfKLQSSDLG 418
Cdd:NF033930 175 -----VAKKKVDEAKKKVEEAKKKVE-----AEEAEIEKLQNEEVALEAKIA--ELENQVDNL---EKELA-EIDESDSE 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 419 --VKQ--KSELNSRLEEKTNQMAATIKQLEQRLRQAE-RSRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRNQLELEL 493
Cdd:NF033930 239 dyIKEglRAPLESELDAKQAKLAKKQTELEKLLDSLDpEGKTQDELDKEAAEEELSKKIDELDNEVAKLEKEVSDLENSD 318
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114594366 494 ----KQEKErRLQNDRSIPGRGSQKSESKMDgkhKMQEEnvkLKKPLEESHRLQPHPMDEQ 550
Cdd:NF033930 319 nnvaDYYKE-ALEKDLATKKAELEKTQKDLD---KALNE---LGPDGDEEETPAPAPQPEQ 372
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
573-608 2.72e-04

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: 39.34  E-value: 2.72e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 114594366 573 KNVCKNCSGTFCDACSTNELPLPSSIKLE--RVCNPCH 608
Cdd:cd15733   23 KHHCRNCGNVFCADCSNYKLPIPDEQLYDpvRVCNSCY 60
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
256-408 3.36e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 3.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   256 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNT-------KLTEELAVANNRIITLQEEMERvkeessyiLESNR 328
Cdd:TIGR02168  345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrskvaQLELQIASLNNEIERLEARLER--------LEDRR 416
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   329 KGPKQDRTAEGQALSEARkhlKEETQLRLD-VEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHE 407
Cdd:TIGR02168  417 ERLQQEIEELLKKLEEAE---LKELQAELEeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493

                   .
gi 114594366   408 L 408
Cdd:TIGR02168  494 L 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
254-495 3.85e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 3.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   254 DGQITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyiLESNRKGPKQ 333
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE----LEELESRLEE 376
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   334 DRTAEGQALSEARKHLKEETQLRLDV---EKELEMQISMRQEMELAMKMLEKDVCEKQDALVSlrQQLDDLRALKHELaf 410
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNEIerlEARLERLEDRRERLQQEIEELLKKLEEAELKELQ--AELEELEEELEEL-- 452
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   411 klqssdlgVKQKSELNSRLEEKTNQmaatIKQLEQRLRQAErsRQSAELDNRLfkqdfgDKINSLQLEVEELTRQRNQLE 490
Cdd:TIGR02168  453 --------QEELERLEEALEELREE----LEEAEQALDAAE--RELAQLQARL------DSLERLQENLEGFSEGVKALL 512

                   ....*
gi 114594366   491 LELKQ 495
Cdd:TIGR02168  513 KNQSG 517
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ...
260-506 4.70e-04

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: 43.34  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  260 ILDQKNYV-EELNRHLNATVNNLQAKVDaLEKSNTKLTEELAVANNRIITLQEEMERVKEESSyILESNRKGPKQDRTAE 338
Cdd:COG3096   263 ISEATNYVaADYMRHANERRVHLDQALE-FRRELYTSRQQLAAEQYRHVDMSRELAELNGAEG-DLEADYQAASDHLNLV 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  339 GQALSEARKHLK-----EETQLRLDVEKELEMQISMRQ-EMELAMKMLEKDVCEKQDALVSLRQQLD--DLRALKHELAF 410
Cdd:COG3096   341 QTALRQQEKIERyqadlEELTIRLEEQNEVVEEANERQeENEARAEAAELEVDELKSQLADYQQALDvqQTRAIQYQQAI 420
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  411 K--------LQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRLFKQDFGDKINSLQLEV-EE 481
Cdd:COG3096   421 AalerakelCHLPDLTADSAEEWLETFQAKEEEATEKLLSLEQKMSMAQAAHSQFEQAYQLVVAIAGELARSEAWDVaRE 500
                         250       260       270
                  ....*....|....*....|....*....|....
gi 114594366  482 LTR----QRNQLE----LELKQ-EKERRLQNDRS 506
Cdd:COG3096   501 LLRegpdQRHLAEqvqpLRMRLsELEQRLRQQQS 534
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
268-498 5.05e-04

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


Pssm-ID: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 43.24  E-value: 5.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   268 EELNRHLNATVNNLQAKVDALEKsntKLTEELAvANNRI----ITLQEEMERVKEESSYILESNRKGPKQDRTAEgQALS 343
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEE---QLEEEEA-ARQKLqlekVTTEAKIKKLEEDILLLEDQNSKLSKERKLLE-ERIS 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   344 EARKHLKEE-------TQLRL-------DVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 409
Cdd:pfam01576  163 EFTSNLAEEeekvkslNKLKNkheamisDLEDRLKKEEKGRQELEKAKRKLDGESTDLQEQIAELQAQIEELRAQLAKKE 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   410 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRlfkqDFGDKINSLQLEVEE-LTRQRNQ 488
Cdd:pfam01576  243 EELQAALARLEEEGAQKNNALKKLRELQAQIAELQEDLESERAARAKAEKQRR----DLGEELEALKTELEDtLDSTAAQ 318
                          250
                   ....*....|
gi 114594366   489 LELELKQEKE 498
Cdd:pfam01576  319 QELRSKREQE 328
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
267-501 6.90e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 42.78  E-value: 6.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  267 VEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQ--DRTAEGQALSE 344
Cdd:COG1196   286 LQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLlaELEEAKEELEE 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  345 ARKHLKEETQLRLDVEKElEMQISMRQEMELAMKM--LEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQK 422
Cdd:COG1196   366 KLSALLEELEELFEALRE-ELAELEAELAEIRNELeeLKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEEL 444
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  423 SELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAEldnrlfkqdfgDKINSLQLEVEEL--TRQRNQLELELKQEKERR 500
Cdd:COG1196   445 NEELEELEEQLEELRDRLKELERELAELQEELQRLE-----------KELSSLEARLDRLeaEQRASQGVRAVLEALESG 513

                  .
gi 114594366  501 L 501
Cdd:COG1196   514 L 514
COG5281 COG5281
Phage-related minor tail protein [Mobilome: prophages, transposons];
234-541 7.73e-04

Phage-related minor tail protein [Mobilome: prophages, transposons];


Pssm-ID: 227606 [Multi-domain]  Cd Length: 833  Bit Score: 42.70  E-value: 7.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 234 GVIDFSMYLKDGNSSKGTEGDGQITAILDQKNYVEELNRHLnATVNNLQAKVDALEKSNTKLTEELavaNNRIITLQEEM 313
Cdd:COG5281  311 AMDDRTARVKENMGTLETAWDALADAAKKMWDAVLGIGRED-KQAALLAAKLAAEKLARVTAQGAL---NARLKLAQDDL 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 314 ERVKEE-SSYILESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVcEKQDALV 392
Cdd:COG5281  387 TQAELNyAAADQAANQEGALNAREDEAEVLSTQEERRDILKNLLADAEKRTARQEELNKALAKAKILQADKA-AKAYQED 465
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 393 SLRQQLDDLR--------------ALKHELAFKLQSSDL-GVKQKSELNSRLEEKTNQMAATIKqLEQRLRQaeRSRQSA 457
Cdd:COG5281  466 ILQREAQSRGktaaaersqeqmtaALKALLAFQQQIADLsGAKEKASDQKSLLWKAEEQYALLK-EEAKQRQ--LQEQKA 542
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 458 ELDnrlfkqdfgdkinsLQLEVEELTRqrnQLELELKQEKERRLQndrSIPGRGSQKSESKMDGKHKMQEENVKLKKPLE 537
Cdd:COG5281  543 LLE--------------HKKETLEYTS---QLAELLDQQADRFEL---SAQAAGSQKERGSDLYREALAQNAAALNKALN 602

                 ....
gi 114594366 538 ESHR 541
Cdd:COG5281  603 ELAA 606
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
340-507 9.70e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 42.39  E-value: 9.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  340 QALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGV 419
Cdd:COG1196   674 EELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEEL 753
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  420 KQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQ---SAELDNRLFKQDFGDKINSLQLEVEELTRQRNQLELELKQE 496
Cdd:COG1196   754 EELQERLEELEEELESLEEALAKLKEEIEELEEKRQalqEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEEL 833
                         170
                  ....*....|.
gi 114594366  497 KERRLQNDRSI 507
Cdd:COG1196   834 EEEIEELEEKL 844
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
256-533 1.09e-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: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  256 QITAILDQKNYVEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEEssyilesnrkgpkqdR 335
Cdd:COG1196   268 EIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEK---------------I 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  336 TAEGQALSEARKHLKEETQLRLDVEKELEmqiSMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS 415
Cdd:COG1196   333 EALKEELEERETLLEELEQLLAELEEAKE---ELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESL 409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  416 DLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAEldnrlfkqdfgDKINSLQLEVEELTRQRNQLELELkQ 495
Cdd:COG1196   410 EERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELE-----------EQLEELRDRLKELERELAELQEEL-Q 477
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 114594366  496 EKERRLQNDRSIPGRGSQKSESKMDGKHKMQEENVKLK 533
Cdd:COG1196   478 RLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLP 515
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
573-613 1.30e-03

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: 37.71  E-value: 1.30e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 114594366 573 KNVCKNCSGTFCDACSTNELPLPSSIKLERVCNPCHKHLMK 613
Cdd:cd15739   26 KHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCHTLLVK 66
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
270-450 1.31e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 41.96  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  270 LNRHLNATVNNLQAKVDALEK--SNTKLTEELAVANNRII----TLQEEMERVKEESSYI----------------LESN 327
Cdd:PRK10929   80 LSAELRQQLNNERDEPRSVPPnmSTDALEQEILQVSSQLLeksrQAQQEQDRAREISDSLsqlpqqqtearrqlneIERR 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  328 RKGPKQDRTAEGQALSEARKhlKEETQLRLDVEkELEM-QISM--RQEM-ELAMKMLEKDVCEKQDALVSLRQQLDDLRA 403
Cdd:PRK10929  160 LQTLGTPNTPLAQAQLTALQ--AESAALKALVD-ELELaQLSAnnRQELaRLRSELAKKRSQQLDAYLQALRNQLNSQRQ 236
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 114594366  404 LKHELAFKL------QSSDL--GVKQKSELNSRLEEKTNQMAATIKQLEQRLRQA 450
Cdd:PRK10929  237 REAERALEStellaeQSGDLpkSIVAQFKINRELSQALNQQAQRMDLIASQQRQA 291
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
268-500 1.47e-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: 41.54  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  268 EELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTAEG-------- 339
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKkikelekq 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  340 -------------QALSEARKHLKEETQLRLDVEKELEMQISMRQ----EMELAMKMLEKDVCEKQDALVSLRQQL---- 398
Cdd:TIGR04523 290 lnqlkseisdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNkiisQLNEQISQLKKELTNSESENSEKQRELeekq 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  399 DDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMaatiKQLEQRLRQAERSRQSAELDNRLFKQDfgdkINSLQLE 478
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN----QQKDEQIKKLQQEKELLEKEIERLKET----IIKNNSE 441
                         250       260
                  ....*....|....*....|..
gi 114594366  479 VEELTRQRNQLELELKQEKERR 500
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTR 463
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
256-557 1.50e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.49  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   256 QITAILDQknyvEELNRHLNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILesnrkgpkQDR 335
Cdd:TIGR00618  387 QKTTLTQK----LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA--------QCE 454
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   336 TAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEME---LAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKL 412
Cdd:TIGR00618  455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLarlLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGE 534
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   413 QSSDLGVKQKSELNSRLEEKTNQmAATIKQLEQRLRQAE------RSRQSAELDNRLFKQDFGDKINSLQLEVEELTRQR 486
Cdd:TIGR00618  535 QTYAQLETSEEDVYHQLTSERKQ-RASLKEQMQEIQQSFsiltqcDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114594366   487 NQLELELKQEKerrlQNDRSIPGRGSQKSESKMDGKHKMQEENVKLKKPLEESH----RLQPHPMDEQDQLLLSE 557
Cdd:TIGR00618  614 QHALLRKLQPE----QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHalsiRVLPKELLASRQLALQK 684
PRK12704 PRK12704
phosphodiesterase; Provisional
420-503 1.51e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 420 KQKSELNSRLEEKTNQmaatIKQLEQRLRQAER--SRQSAELDNRlfKQDFGDKINSLQLEVEELTRQRNQLElELKQEK 497
Cdd:PRK12704  68 KLRNEFEKELRERRNE----LQKLEKRLLQKEEnlDRKLELLEKR--EEELEKKEKELEQKQQELEKKEEELE-ELIEEQ 140

                 ....*.
gi 114594366 498 ERRLQN 503
Cdd:PRK12704 141 LQELER 146
M_group_A_cterm NF033777
M protein C-terminal domain; M protein (emm) is an important virulence protein and ...
267-409 1.78e-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: 40.20  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 267 VEELNRHLNATVNNLQAKVDALEKSNTKLTEELAvannriiTLQEEMERVKEESSyILESNRKGPKQDRTAEGQALSEAR 346
Cdd:NF033777   7 LEEQNKISEASRKGLRRDLDASREAKKQVEKDLA-------NLTAELDKVKEEKQ-ISDASRQGLRRDLDASREAKKQVE 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114594366 347 KHLKEETQLRLDVEKelemqisMRQEMELAMKMLEKDVCEKQDALVSlrqqldDLRALKHELA 409
Cdd:NF033777  79 KALEEANSKLAALEK-------LNKELEESKKLTEKEKAELQAKLEA------EAKALKEQLA 128
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
562-608 1.95e-03

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: 36.71  E-value: 1.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 114594366 562 CQLCQEDGSLTKNV--CKNCSGTFCDACSTNELPLPS-SIKLERVCNPCH 608
Cdd:cd15749    2 CFGCAAKFSLFKKEcgCKNCGRSFCKGCLTFSAVVPRkGNQKQKVCKQCH 51
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
560-608 2.13e-03

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: 36.58  E-value: 2.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 114594366 560 QVCQLCQEdgslTK-NV------CKNCSGTFCDACSTNELPLPS-SIKLERVCNPCH 608
Cdd:cd15717    9 PVCMHCKK----TKfTAinrrhhCRKCGAVVCGACSSKKFLLPHqSSKPLRVCDTCY 61
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
268-497 2.28e-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: 41.26  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   268 EELNRHLNATVNNLQA----KVDALEKSNTKLtEELavannRIITLQEEmeRVKEESSYIL-----ESNRKGPKQDRTAE 338
Cdd:pfam15921  141 EDLRNQLQNTVHELEAakclKEDMLEDSNTQI-EQL-----RKMMLSHE--GVLQEIRSILvdfeeASGKKIYEHDSMST 212
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   339 ------GQALSEARKHLKEETQLR----LDVEKELEMQISMRQ-EMELAMKM----LEKDVCEKQDALVSLRQQLDDLRA 403
Cdd:pfam15921  213 mhfrslGSAISKILRELDTEISYLkgriFPVEDQLEALKSESQnKIELLLQQhqdrIEQLISEHEVEITGLTEKASSARS 292
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   404 LKHELAFKLQssdLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSA--ELDNRL----------------FK 465
Cdd:pfam15921  293 QANSIQSQLE---IIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKieELEKQLvlanseltearterdqFS 369
                          250       260       270
                   ....*....|....*....|....*....|..
gi 114594366   466 QDFGDKINSLQLEVEELTRQRNQLELELKQEK 497
Cdd:pfam15921  370 QESGNLDDQLQKLLADLHKREKELSLEKEQNK 401
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
293-500 2.47e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 2.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   293 TKLTEELAVANNRIITLQEEMERVKEessyIL-ESNRKGPKQDRTAEgqaLSEARKHLKEE-TQLRLDVE-KELEMQISM 369
Cdd:TIGR02168  168 SKYKERRKETERKLERTRENLDRLED----ILnELERQLKSLERQAE---KAERYKELKAElRELELALLvLRLEELREE 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   370 RQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKtnqmaatIKQLEQRLRQ 449
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ-------KQILRERLAN 313
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 114594366   450 AERSRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRNQLELELKQEKERR 500
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
268-503 3.46e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 268 EELNRHLNATVNNLQAKVDALEKSntklTEELAVANNRIITLQEEMERVKEESSYILESNRKGPKQDRTAEGQALSEARK 347
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKE----LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEP 599
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 348 HLKEETQLRlDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKlqssdlgvkqkselns 427
Cdd:PRK03918 600 FYNEYLELK-DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE---------------- 662
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 114594366 428 RLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRLFKQDFgDKINSLQLEVEELTRQRNQLElELKqEKERRLQN 503
Cdd:PRK03918 663 ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL-EEREKAKKELEKLEKALERVE-ELR-EKVKKYKA 735
xseA PRK00286
exodeoxyribonuclease VII large subunit; Reviewed
376-499 3.47e-03

exodeoxyribonuclease VII large subunit; Reviewed


Pssm-ID: 234714  Cd Length: 438  Bit Score: 40.18  E-value: 3.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 376 AMKMLEKDVCEKQDALVSLRQQLddLRALKHELAFKLQSSDLgvkqkseLNSRL-----EEKTNQMAATIKQLEQRLRQA 450
Cdd:PRK00286 254 AAELAVPDRAELLQRLQQLQQRL--ARAMRRRLEQKRQRLDQ-------LARRLkfqspERLLAQQQQRLDRLQQRLQRA 324
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 114594366 451 ------ERSRQSAELDNRLFKQDFGDKINSLQLEVEEL-TRQRNQLELELKQEKER 499
Cdd:PRK00286 325 lerrlrLAKQRLERLSQRLQQQNPQRRIERAQQRLEQLeQRLRRAMRRQLKRKRQR 380
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
562-607 3.69e-03

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: 36.00  E-value: 3.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 114594366 562 CQLCQEDGS--LTKNVCKNCSGTFCDACSTNELPLPSSIKLERVCNPC 607
Cdd:cd15726   10 CLDCKSEFSwmVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKAC 57
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
302-503 5.65e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 5.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   302 ANNRIITLQEEMERvkeeSSYILESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLE 381
Cdd:TIGR02168  643 PGYRIVTLDGDLVR----PGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLR 718
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   382 KDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDN 461
Cdd:TIGR02168  719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 114594366   462 RLFKQDFGDKINSLQLEVEELTRQRNQLELELKQ--EKERRLQN 503
Cdd:TIGR02168  799 KALREALDELRAELTLLNEEAANLRERLESLERRiaATERRLED 842
PLN02939 PLN02939
transferase, transferring glycosyl groups
282-553 6.36e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 39.50  E-value: 6.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 282 QAKVDALEKSNTKLTEELAvannriitLQEEMErvkeessyILESNrkgpkqdrtaegqaLSEARKHLKEETQLRLDVEK 361
Cdd:PLN02939 149 QARLQALEDLEKILTEKEA--------LQGKIN--------ILEMR--------------LSETDARIKLAAQEKIHVEI 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 362 ELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQ----LDDLRALKHELafklqssdLGVKQKSELNSRLEEKTNQMA 437
Cdd:PLN02939 199 LEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEEnmllKDDIQFLKAEL--------IEVAETEERVFKLEKERSLLD 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 438 ATIKQLEQRLRQAersrQSAELDNRLFKQD-FGDKINSLQLEVEELTRQRNQLELELKQEKERRLQNDR---SI-PGRGS 512
Cdd:PLN02939 271 ASLRELESKFIVA----QEDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKleaSLkEANVS 346
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 114594366 513 QKSESKMDgkhkMQEENVKLkkpLEESHRLQPHPMDEQDQL 553
Cdd:PLN02939 347 KFSSYKVE----LLQQKLKL---LEERLQASDHEIHSYIQL 380
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
264-552 6.37e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 39.64  E-value: 6.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   264 KNYVEELNRHLNATVNNLQAKVDALEKSNTKltEELAVANNRIITLqeeMERVKEEssyiLESNRKgpkqdRTAEGQALS 343
Cdd:TIGR00606  750 RNKLQKVNRDIQRLKNDIEEQETLLGTIMPE--EESAKVCLTDVTI---MERFQME----LKDVER-----KIAQQAAKL 815
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   344 EARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEkdvcEKQDALVSLRQQLDDLRALKHELAFKLQ-------SSD 416
Cdd:TIGR00606  816 QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQ----DQQEQIQHLKSKTNELKSEKLQIGTNLQrrqqfeeQLV 891
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   417 LGVKQKSELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSAELDNRLFKqdfgDKINSLQLEVEELTRQRNQLELELKQE 496
Cdd:TIGR00606  892 ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQ----DKVNDIKEKVKNIHGYMKDIENKIQDG 967
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 114594366   497 KERRLQNdrsipgrgsqkSESKMDGKHKMQEENVKLKKPLEESHRLQPHPMDEQDQ 552
Cdd:TIGR00606  968 KDDYLKQ-----------KETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKI 1012
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
274-494 6.65e-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: 39.62  E-value: 6.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  274 LNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEES----SYILESNRKGPKQDRTA------------ 337
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIknleSQINDLESKIQNQEKLNqqkdeqikklqq 419
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  338 EGQALSEARKHLKEETQLRLDVEKELEMQISmrqEMELAMKMLEKDVCEKQDALVSLRQQLD----DLRALKHELAFKLQ 413
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDS---VKELIIKNLDNTRESLETQLKVLSRSINkikqNLEQKQKELKSKEK 496
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366  414 SSDLGVKQKSEL---NSRLEEKTNQMAATIKQLEqrLRQAERSRQSAELDNRLFKQDFGDKINSLQLEVEELTRQRNQLE 490
Cdd:TIGR04523 497 ELKKLNEEKKELeekVKDLTKKISSLKEKIEKLE--SEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELK 574

                  ....
gi 114594366  491 LELK 494
Cdd:TIGR04523 575 QTQK 578
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
282-456 6.67e-03

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


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 39.24  E-value: 6.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 282 QAKVDALEKSNTKLTEELAVANNRIITLQEEMERVKEESSYILESnrkgpKQDRTAEGQALSEARKHLKEEtqlRLDVEK 361
Cdd:COG4372  122 RQELAAARQNLAKAQQELARLTKQAQDLQTRLKTLAEQRRQLEAQ-----AQSLQASQKQLQASATQLKSQ---VLDLKL 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 362 ELEmQISmRQEMELAMKmlEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIK 441
Cdd:COG4372  194 RSA-QIE-QEAQNLATR--ANAAQARTEELARRAAAAQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQA 269
                        170
                 ....*....|....*
gi 114594366 442 QLEQRLRQAERSRQS 456
Cdd:COG4372  270 RLEQEVAQLEAYYQA 284
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
267-446 7.38e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.05  E-value: 7.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 267 VEELNRHLNATVNNL----QAKVDA---LEKSNTKLTEELAVANNRIITLQEEMERVKEesSYIL-----ESNRKGPKQ- 333
Cdd:PRK04778 280 AEEKNEEIQERIDQLydilEREVKArkyVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQ--SYTLneselESVRQLEKQl 357
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 334 -----------DRTAEG-QALSEARKHLKE-ETQLRlDVEKElemQISMRQEmelaMKMLEKDvcEKQdalvsLRQQLDD 400
Cdd:PRK04778 358 eslekqydeitERIAEQeIAYSELQEELEEiLKQLE-EIEKE---QEKLSEM----LQGLRKD--ELE-----AREKLER 422
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 114594366 401 LRALKHELAFKLQSSDL-GVKQksELNSRLEEKTNQMAATIKQLEQR 446
Cdd:PRK04778 423 YRNKLHEIKRYLEKSNLpGLPE--DYLEMFFEVSDEIEALAEELEEK 467
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
293-566 7.47e-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: 39.33  E-value: 7.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   293 TKLTEELAVANNRIITLQEEMERVKEESSyilESNRKGPKQDRTAEgQALSEARKHLKEETQLRLDVEKELEMQISMRQE 372
Cdd:pfam15921  281 TGLTEKASSARSQANSIQSQLEIIQEQAR---NQNSMYMRQLSDLE-STVSQLRSELREAKRMYEDKIEELEKQLVLANS 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   373 mELAMKMLEKDVCEKQDALV--SLRQQLDDLRALKHELAFKlqssdlgvkqkSELNSRLEEKTNQMAATIKQLE------ 444
Cdd:pfam15921  357 -ELTEARTERDQFSQESGNLddQLQKLLADLHKREKELSLE-----------KEQNKRLWDRDTGNSITIDHLRrelddr 424
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366   445 ----QRLR----------QAERSRQSAELDNrlfKQDFGDKINSL--QLE---------VEELTRQRNQLELELK----- 494
Cdd:pfam15921  425 nmevQRLEallkamksecQGQMERQMAAIQG---KNESLEKVSSLtaQLEstkemlrkvVEELTAKKMTLESSERtvsdl 501
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 114594366   495 ----QEKERRLQNDRSIPGRGSQKSESKMDGKHKMQEENVKLKKPLEESHRLQPHpMDEQDQLLLSEKPQVCQLCQ 566
Cdd:pfam15921  502 taslQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ-MAEKDKVIEILRQQIENMTQ 576
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
333-499 7.49e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 38.93  E-value: 7.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 333 QDRTAEGQALSEARKHLKEETQLRLDVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHEL---- 408
Cdd:COG4942   31 FSAAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALevqe 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 409 ------------AFKLQSSD----LGVKQKSELNSR-----LEEKTNQMAATIKQLEQRLRQ-----AERSRQSAELDNR 462
Cdd:COG4942  111 reqrrrlaeqlaALQRSGRNpppaLLVSPEDAQRSVrlaiyYGALNPARAERIDALKATLKQlaavrAEIAAEQAELTTL 190
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 114594366 463 LFKQDfgDKINSLQLEVEELTRQRNQLELELKQEKER 499
Cdd:COG4942  191 LSEQR--AQQAKLAQLLEERKKTLAQLNSELSADQKK 225
CwlO1 COG3883
Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown];
274-457 8.37e-03

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


Pssm-ID: 226400 [Multi-domain]  Cd Length: 265  Bit Score: 38.55  E-value: 8.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 274 LNATVNNLQAKVDALEKSNTKLTEELAVANNRIITLQEEM-ERVK------EESSY---ILESNRKGPKQDR-TAEGQAL 342
Cdd:COG3883   64 IQSKIDELQKEIDQSKAEIKKLQKEIAELKENIVERQELLkKRARamqvngTATSYidvILNSKSFSDLISRvTAISVIV 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 343 SEARKHLK--EETQLRL-----DVEKELEMQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELafklqss 415
Cdd:COG3883  144 DADKKILEqqKEDKKSLeekqaALEDKLETLVALQNELETQLNSLNSQKAEKNALIAALAAKEASALGEKAAL------- 216
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 114594366 416 dlgVKQKS-ELNSRLEEKTNQMAATIKQLEQRLRQAERSRQSA 457
Cdd:COG3883  217 ---EEQKAlAEAAAAEAAKQEAAAKAAAQEQAALQAAATAAQP 256
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
274-454 8.49e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 225288  Cd Length: 652  Bit Score: 38.92  E-value: 8.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 274 LNATVNNLQAKVDALEKSNTKLTEELAVAN-NRI-------ITLQEEMERVKEESSyilesnrkgPKQDRTAEGQALSEA 345
Cdd:COG2433  347 LAAAYKAYLAYKPKLEKVERKLPELGIWKDvERIkalvirgYPLAEALSKVKEEER---------PREKEGTEEEERREI 417
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 346 RKHLKEETQLRLDVEKeLEMQIsmrqemelamKMLEKDVCEKQDALVSLRQQLDDLRAlkhELAFKLQSsDLGVKQKSEL 425
Cdd:COG2433  418 TVYEKRIKKLEETVER-LEEEN----------SELKRELEELKREIEKLESELERFRR---EVRDKVRK-DREIRARDRR 482
                        170       180
                 ....*....|....*....|....*....
gi 114594366 426 NSRLEEKTNQMAATIKQLEQRLRQAERSR 454
Cdd:COG2433  483 IERLEKELEEKKKRVEELERKLAELRKMR 511
HEC1 COG5185
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, ...
288-496 8.64e-03

Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227512 [Multi-domain]  Cd Length: 622  Bit Score: 39.19  E-value: 8.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 288 LEKSNTKLTEELAVANNRIIT-LQEEMERVKEESSYILEsnrkgpkqdRTAEGQALSEARKHLKEETQLRLDVEKELEMQ 366
Cdd:COG5185  247 LEDNYEPSEQELKLGFEKFVHiINTDIANLKTQNDNLYE---------KIQEAMKISQKIKTLREKWRALKSDSNKYENY 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 367 IS-MRQEMEL---AMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQ 442
Cdd:COG5185  318 VNaMKQKSQEwpgKLEKLKSEIELKEEEIKALQSNIDELHKQLRKQGISTEQFELMNQEREKLTRELDKINIQSDKLTKS 397
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 114594366 443 LEQRLRQAERSRQSAEldnRLFkQDFGDKINSLQLEVEELTRQRNQLELELKQE 496
Cdd:COG5185  398 VKSRKLEAQGIFKSLE---KTL-RQYDSLIQNITRSRSQIGHNVNDSSLKINIE 447
YloA COG1293
Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains ...
370-534 9.93e-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: 38.91  E-value: 9.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 370 RQEMELAMKMLEKDVC---EKQDALVSLRQqLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQR 446
Cdd:COG1293  230 REALEELLNPLKPNYYykdEKYLDVVPLKA-YADLEKLFNEALDEKFERDKIKQLASELEKKLEKELKKLENKLEKQEDE 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114594366 447 LRQAERSrqsaelDNRLFKQdfGDKINSLQLEVEELTRQRNQLELELKQEKERRLqNDRSIPGRGSQ---KSESKMDGKH 523
Cdd:COG1293  309 LEELEKA------AEELRQK--GELLYANLQLIEEGLKSVRLADFYGNEEIKIEL-DKSKTPSENAQryfKKYKKLKGAK 379
                        170
                 ....*....|.
gi 114594366 524 KMQEENVKLKK 534
Cdd:COG1293  380 VNLDRQLSELK 390
 
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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