NCBI Conserved Domain Search

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

401-513

7.30e-08

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 7.30e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 401 ARREEQAEVS-LQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQ 479
Cdd:COG1196  289 EEYELLAELArLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                         90       100       110
                 ....*....|....*....|....*....|....
gi 282165733 480 EELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHL 513
Cdd:COG1196  369 EAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

FYVE

smart00064

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...

519-564

2.05e-07

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: 48.20 E-value: 2.05e-07

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 282165733   519 ECCVACSKIFGRFSRRYPCRLCGGLLCHACS--------MDYKKRDRCCPPCAQ 564
Cdd:smart00064  11 SNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSskkaplpkLGIERPVRVCDDCYE 64

FYVE

pfam01363

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...

520-564

1.61e-06

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

Pssm-ID: 426221 [Multi-domain] Cd Length: 68 Bit Score: 45.84 E-value: 1.61e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 282165733  520 CCVACSKIFGRFSRRYPCRLCGGLLCHACS---------MDYKKRDRCCPPCAQ 564
Cdd:pfam01363  11 VCMICSKPFTFFRRRHHCRNCGRVFCSACSskkisllpeLGSNKPVRVCDACYD 64

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

397-516

3.02e-06

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

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 3.02e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   397 VTLVARREEQAEVsLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLE---QKQQEAER 473
Cdd:TIGR02168  294 ANEISRLEQQKQI-LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEeleAELEELES 372

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 282165733   474 RDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSSM 516
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415

RUN

smart00593

domain involved in Ras-like GTPase signaling;

101-163

1.25e-05

domain involved in Ras-like GTPase signaling;

Pssm-ID: 214736 [Multi-domain] Cd Length: 64 Bit Score: 42.99 E-value: 1.25e-05

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 282165733   101 GRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFELDL 163
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRDPEEGEQLLGLLVGLSALDFNLPV 63

Lebercilin

pfam15619

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...

410-511

1.89e-05

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.

Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 45.66 E-value: 1.89e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  410 SLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQE--------ERAELQAQLEQKQQEAERRDAMYQE- 480
Cdd:pfam15619  64 RHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKlsedknlaEREELQKKLEQLEAKLEDKDEKIQDl 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 282165733  481 -------------ELGGQRDLVQAMKRRVLELIQEKDRLWQRLQ 511
Cdd:pfam15619 144 erklelenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187

hsdR

PRK11448

type I restriction enzyme EcoKI subunit R; Provisional

405-505

2.30e-05

type I restriction enzyme EcoKI subunit R; Provisional

Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 47.64 E-value: 2.30e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  405 EQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEELGG 484
Cdd:PRK11448  141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKE 220

                          90       100
                  ....*....|....*....|.
gi 282165733  485 QRDlvQAMKRrvLELIQEKDR 505
Cdd:PRK11448  221 ITD--QAAKR--LELSEEETR 237

OmpH

smart00935

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...

424-502

2.27e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.

Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 41.42 E-value: 2.27e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   424 KAEEQAQRQEQLLREQEGELQALREQLSR-----CQEERAELQAQLEQKQQEAERRDAMYQEEL-GGQRDLVQAMKRRVL 497
Cdd:smart00935  22 QLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlSEAAREKKEKELQKKVQEFQRKQQKLQQDLqKRQQEELQKILDKIN 101


                   ....*
gi 282165733   498 ELIQE 502
Cdd:smart00935 102 KAIKE 106

GBP_C

cd16269

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...

406-503

1.43e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.

Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.02 E-value: 1.43e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 406 QAEVSLQDEIKSLRLgLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAE-LQAQLEQKQQEAERR-DAMYQEELG 483
Cdd:cd16269  188 QADQALTEKEKEIEA-ERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRqLKEKMEEERENLLKEqERALESKLK 266

                         90       100
                 ....*....|....*....|
gi 282165733 484 GQRDLVQAMKRRVLELIQEK 503
Cdd:cd16269  267 EQEALLEEGFKEQAELLQEE 286

Name

Accession

Description

Interval

E-value

RUN_RUFY4

cd17697

RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ...

13-161

8.90e-87

Pssm-ID: 439059 Cd Length: 150 Bit Score: 265.51 E-value: 8.90e-87

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  13 DLRAAVSAILQGYGDGQG-PVTDTSAELHRLCGCLELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPIHFVRSQ 91
Cdd:cd17697    1 KDLQASIAELQKDQEEQQlPITDGSPELHRLCARLEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNST 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  92 DKLKTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFEL 161
Cdd:cd17697   81 DKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNPELTGEWYYARSPFLSPELRSDILDSLYELNGVNFDL 150

RUN_FYCO1

cd17698

RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...

9-161

8.67e-55

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

Pssm-ID: 439060 Cd Length: 158 Bit Score: 182.59 E-value: 8.67e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   9 KVTKDLRAAVSAILQGYGDGQGPVTDTSAELHRLCGCLELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPIHFV 88
Cdd:cd17698    6 KIIRDLQDCVTELKKEFEETGEPITDDSTTLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFCECLAKVKGLNDGIRFV 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 282165733  89 RSQDKLKTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFEL 161
Cdd:cd17698   86 KSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDWYYPRSVFLNHKYSSDIINSLYDLNEVQFDL 158

RUN_RUFY4_like

cd17682

RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ...

13-161

3.62e-45

RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil domain-containing protein 1 (FYCO1), and similar proteins; The family includes RUFY4 and FYCO1. RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. Both RUFY4 and FYCO1 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.

Pssm-ID: 439044 Cd Length: 150 Bit Score: 156.62 E-value: 3.62e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  13 DLRAAVSAILQGYGDgqgPVTDTSAELHRLCGCLELLLQFDQKEQKSFLGPRKDYWDFLCTALRR----QRGNMEPIHFV 88
Cdd:cd17682    1 DLKGCVLDLKSEFGE---ITDPDNPYLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEELLKKlnkiPKSLSDAVKFV 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 282165733  89 RSQDKLKTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFEL 161
Cdd:cd17682   78 KSCKKVKTNQGRGRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEILSEILLSLLYQLNEINFDL 150

RUN

cd17671

RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...

17-161

1.76e-28

Pssm-ID: 439038 Cd Length: 154 Bit Score: 110.98 E-value: 1.76e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  17 AVSAILQGYGDGQG-------PVTDTSAELHRLCGCLELLLQFDQKEqKSFLGPRKDYWDFLCTALRRQRGN--MEPIHF 87
Cdd:cd17671    2 AVKELLESFADNGEaddsaalTLTDDDPVVGRLCAALEAILSHGLKP-KRFGGGKVSFWDFLEALEKLLPAPslKQAIRD 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 282165733  88 VRSQDKLKTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFEL 161
Cdd:cd17671   81 INSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRDPEEAELFLSLLVGLSSLDFNL 154

RUN_RUFY1_like

cd17681

RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ...

29-161

1.23e-13

RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1, RUFY2, and RUFY3. RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. RUFY1, RUFY2, and RUFY3 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.

Pssm-ID: 439043 Cd Length: 155 Bit Score: 68.75 E-value: 1.23e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  29 QGPVTDTSAELHRLCGCLELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPIHFVRSQDKLKTPLGKGRAFIRFC 108
Cdd:cd17681   24 GRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEITASVRDLPGIKTPLGRARAWLRLA 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 282165733 109 LARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEdILDSLYALNGVAFEL 161
Cdd:cd17681  104 LMQKKLADYFRALIENKDLLSEFYEPGALMMSEEAVV-IAGLLVGLNVIDCNL 155

FYVE_RUFY4

cd15745

FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...

520-562

3.93e-12

Pssm-ID: 277284 [Multi-domain] Cd Length: 52 Bit Score: 60.98 E-value: 3.93e-12

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 282165733 520 CCVACSKIFGRFSRRYPCRLCGGLLCHACSMDYK--------KRDRCCPPC 562
Cdd:cd15745    1 ACAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLvlsvpdtcIYLRVCKTC 51

RUN_RUNDC3

cd17684

RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ...

15-161

4.54e-11

RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 contains two isoforms, RUNDC3A and RUNDC3B. RUNDC3A, also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. RUNDC3B, also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. Both RUNDC3A and RUNDC3B contain a RUN domain.

Pssm-ID: 439046 Cd Length: 150 Bit Score: 61.26 E-value: 4.54e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  15 RAAVSAILQGYGDGqgPVTDTSAELHRLCGCLELLLQFDQKEQKSFLG--PRKDYWDFLCTALRRQRGNMepIHFVRSQD 92
Cdd:cd17684    7 RLSVKSLIDKACLE--TIDDSSEELINFAAILEQILSHRLKPVKPWYGseEPRTFWDYIRVACKKVPQNC--IASIEQME 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165733  93 KLKTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLcperQED---ILDSLYALNGVAFEL 161
Cdd:cd17684   83 NIKSPKAKGRAWIRVALMEKRLSEYLSTALKQTRLTRNFYQDGAIML----SEDatvLCGMLIGLNAIDFSF 150

FYVE_like_SF

cd00065

FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...

520-563

4.06e-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: 52.53 E-value: 4.06e-09

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 282165733 520 CCVACSKIFGRFSRRYPCRLCGGLLCHACS--------MDYKKRDRCCPPCA 563
Cdd:cd00065    1 RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSskklplpsFGSGKPVRVCDSCY 52

RUN

pfam02759

RUN domain; This domain is present in several proteins that are linked to the functions of ...

41-163

9.90e-09

Pssm-ID: 460679 Cd Length: 134 Bit Score: 53.82 E-value: 9.90e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   41 RLCGCLELLLQ------FDQKEQKSFLGPRKDYWDFL------CTA---LRRQRGNMEPIHfvrsqdKLKTPLGKGRAFI 105
Cdd:pfam02759   1 QLCAALEALLShglkrsSLLILRAAGLLPERSFWALLervgklVPPaeeLLSSVQELEQIH------TPYSPDGRGRAWI 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 282165733  106 RFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFELDL 163
Cdd:pfam02759  75 RLALNEKLLDQWLKLLLSNKELLSEYYEPWALLADPEFGEILLGLLVGLSALDFNLCL 132

RUN1_DENND5

cd17677

RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 ...

28-159

3.01e-08

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

Pssm-ID: 439039 Cd Length: 183 Bit Score: 53.56 E-value: 3.01e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  28 GQGPVTDTSAE----LHRLCGCLELL----LQFDQKeqKSFLgprkdyWDFLCTAL-RRQRGNMEPIHF------VRSQD 92
Cdd:cd17677   37 GHGEVNITGVEentlIASLCDLLERIwshgLQTKQG--KSAL------WSHLLAYQeNEERLKPLPESLlfdmknVQNMK 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 282165733  93 KLKTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAF 159
Cdd:cd17677  109 EIKTDVGYARAWIRLALEKKLLSKHLKTLLSNQDLLRSLYKRYAFLRCEDEREQFLYHLLSLNAVDY 175

RUN_RUNDC3B

cd17700

RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ...

32-159

4.43e-08

RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN domain-containing protein 3B (RUNDC3B), also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. RUNDC3B contains a RUN domain.

Pssm-ID: 439062 Cd Length: 151 Bit Score: 52.66 E-value: 4.43e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  32 VTDTSAELHRLCGCLELLLQFDQKEQKSFLG---PRKdYWDFLCTALRRQRGNMepIHFVRSQDKLKTPLGKGRAFIRFC 108
Cdd:cd17700   22 IDDSSPEFVNFAAILEQILSHRLKGQVTWFGyesPRS-FWDYIRVACSKVPHNC--ICSIENMENVSSSRAKGRAWIRVA 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 282165733 109 LARGQLAEALQLCLLNSELTREWYgPRSPLLCPERQEDILDSLYALNGVAF 159
Cdd:cd17700   99 LMEKRLSEYISTALRDFKTTRRFY-EDGAIVLGEEANMLAGMLLGLNAIDF 148

Smc

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

401-513

7.30e-08

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 7.30e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 401 ARREEQAEVS-LQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQ 479
Cdd:COG1196  289 EEYELLAELArLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                         90       100       110
                 ....*....|....*....|....*....|....
gi 282165733 480 EELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHL 513
Cdd:COG1196  369 EAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

Smc

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

392-511

9.77e-08

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 9.77e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 392 QVQTEVTLVARREEQAEvsLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQ-------- 463
Cdd:COG1196  262 LAELEAELEELRLELEE--LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEleeleeel 339

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 282165733 464 --LEQKQQEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQ 511
Cdd:COG1196  340 eeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

COG4913

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

376-537

1.60e-07

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 1.60e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  376 VLQGHATKEDSTVENPQVQTEvtLVARREEQAEVSL-QDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQ 454
Cdd:COG4913   649 ALQRLAEYSWDEIDVASAERE--IAELEAELERLDAsSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  455 EERAELQAQLEQKQQEAERR-----DAMYQEELGGQ--RDLVQAMKRRVLELIQEKDRLWQRLQhlssmapeccvacsKI 527
Cdd:COG4913   727 EELDELQDRLEAAEDLARLElrallEERFAAALGDAveRELRENLEERIDALRARLNRAEEELE--------------RA 792

                         170
                  ....*....|
gi 282165733  528 FGRFSRRYPC 537
Cdd:COG4913   793 MRAFNREWPA 802

FYVE

smart00064

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...

519-564

2.05e-07

Pssm-ID: 214499 [Multi-domain] Cd Length: 68 Bit Score: 48.20 E-value: 2.05e-07

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 282165733   519 ECCVACSKIFGRFSRRYPCRLCGGLLCHACS--------MDYKKRDRCCPPCAQ 564
Cdd:smart00064  11 SNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSskkaplpkLGIERPVRVCDDCYE 64

Smc

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

403-517

3.66e-07

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 3.66e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 403 REEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEEL 482
Cdd:COG1196  299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 282165733 483 GGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSSMA 517
Cdd:COG1196  379 EELEELAEELLEALRAAAELAAQLEELEEAEEALL 413

FYVE_FYCO1

cd15726

FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...

521-563

7.19e-07

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

Pssm-ID: 277265 [Multi-domain] Cd Length: 58 Bit Score: 46.40 E-value: 7.19e-07

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 282165733 521 CVACSKIFGRFSRRYPCRLCGGLLCHACSMDY------KKRDRCCPPCA 563
Cdd:cd15726   10 CLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYvltahgGKKERCCKACF 58

Smc

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

403-513

7.34e-07

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 7.34e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 403 REEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQ---LEQKQQEAERRDAMYQ 479
Cdd:COG1196  341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQleeLEEAEEALLERLERLE 420

                         90       100       110
                 ....*....|....*....|....*....|....
gi 282165733 480 EELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHL 513
Cdd:COG1196  421 EELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

402-497

8.46e-07

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 8.46e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 402 RREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQE-AERRDAMYQ- 479
Cdd:COG4942   37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElAELLRALYRl 116

                         90       100
                 ....*....|....*....|....
gi 282165733 480 ------EELGGQRDLVQAMKRRVL 497
Cdd:COG4942  117 grqpplALLLSPEDFLDAVRRLQY 140

Smc

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

392-515

1.24e-06

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.24e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 392 QVQTEVTLVARREEQAEVSLQD---EIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQ 468
Cdd:COG1196  243 ELEAELEELEAELEELEAELAEleaELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 282165733 469 QE---AERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSS 515
Cdd:COG1196  323 EElaeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

FYVE_RBNS5

cd15716

FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ...

515-562

1.25e-06

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

Pssm-ID: 277256 [Multi-domain] Cd Length: 61 Bit Score: 45.80 E-value: 1.25e-06

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 282165733 515 SMAPECCVaCSKIFGRFSRRYPCRLCGGLLCHACSMDYKKRDRCCPPC 562
Cdd:cd15716    8 SDVPFCPD-CGKKFNLARRRHHCRLCGSIMCNKCSQFLPLHIRCCHHC 54

FYVE

pfam01363

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...

520-564

1.61e-06

Pssm-ID: 426221 [Multi-domain] Cd Length: 68 Bit Score: 45.84 E-value: 1.61e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 282165733  520 CCVACSKIFGRFSRRYPCRLCGGLLCHACS---------MDYKKRDRCCPPCAQ 564
Cdd:pfam01363  11 VCMICSKPFTFFRRRHHCRNCGRVFCSACSskkisllpeLGSNKPVRVCDACYD 64

RUN_RUFY2

cd17695

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

46-155

1.71e-06

RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. This model represents the RUN domain of RUFY2.

Pssm-ID: 439057 Cd Length: 156 Bit Score: 48.05 E-value: 1.71e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  46 LELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPIHFVRSQDKLKTPLGKGRAFIRFCLARGQLAEALQLCLLNS 125
Cdd:cd17695   41 MEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIAASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRR 120

                         90       100       110
                 ....*....|....*....|....*....|
gi 282165733 126 ELTREWYgPRSPLLCPERQEDILDSLYALN 155
Cdd:cd17695  121 DLLSEFY-EYHALMMEEEGAVIVGLLVGLN 149

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

397-516

3.02e-06

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 3.02e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   397 VTLVARREEQAEVsLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLE---QKQQEAER 473
Cdd:TIGR02168  294 ANEISRLEQQKQI-LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEeleAELEELES 372

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 282165733   474 RDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSSM 516
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415

Smc

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

404-513

3.47e-06

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 3.47e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 404 EEQAEV-----SLQDEIKSLRLGLR------------KAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQ 466
Cdd:COG1196  206 ERQAEKaeryrELKEELKELEAELLllklreleaeleELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE 285

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 282165733 467 KQQ---EAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHL 513
Cdd:COG1196  286 AQAeeyELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335

RUN1_DENND5B

cd17691

RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ...

49-159

4.35e-06

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

Pssm-ID: 439053 [Multi-domain] Cd Length: 206 Bit Score: 47.74 E-value: 4.35e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  49 LLQFDQKEQKS--------FLGPRKDYWDFLCTALRRQRGNMEPIHFVRSQDKLKTPLGKGRAFIRFCLARGQLAEALQL 120
Cdd:cd17691   80 LLHFQEREEKQehvaespvANGLERRKSETGVNLPTLRVSLIQDMRHIQNMSEIKTDVGRARAWIRLSLEKKLLSQHLKQ 159

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 282165733 121 CLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAF 159
Cdd:cd17691  160 LLSNQALTKKLYKRYAFLRCEEEKEQFLYHLLSLNAVDY 198

HlpA

COG2825

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...

426-502

5.86e-06

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 46.75 E-value: 5.86e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 426 EEQAQRQEQLLREQEGELQALREQLSR-----CQEERAELQAQLEQKQQEAERRDAMYQEELGG-QRDLVQAMKRRVLEL 499
Cdd:COG2825   49 EKEFKKRQAELQKLEKELQALQEKLQKeaatlSEEERQKKERELQKKQQELQRKQQEAQQDLQKrQQELLQPILEKIQKA 128


                 ...
gi 282165733 500 IQE 502
Cdd:COG2825  129 IKE 131

RUN_RUFY3

cd17696

RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...

37-155

6.75e-06

RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. This model represents the RUN domain of RUFY3.

Pssm-ID: 439058 Cd Length: 156 Bit Score: 46.53 E-value: 6.75e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  37 AELHRLCGCLELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPIHFVRSQDKLKTPLGKGRAFIRFCLARGQLAE 116
Cdd:cd17696   32 APLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSE 111

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 282165733 117 ALQLCLLNSELTREWYGPRSpLLCPERQEDILDSLYALN 155
Cdd:cd17696  112 YMKALINRKDLLSEFYEPNA-LMMEEEGAIIAGLLVGLN 149

Smc

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

394-513

7.00e-06

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 7.00e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 394 QTEVTLVARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRcQEERAELQAQLEQKQQEAER 473
Cdd:COG1196  350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA-EEALLERLERLEEELEELEE 428

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 282165733 474 RDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHL 513
Cdd:COG1196  429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

Smc

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

394-506

9.94e-06

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 9.94e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 394 QTEVTLVARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAER 473
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                         90       100       110
                 ....*....|....*....|....*....|...
gi 282165733 474 RDAMYQEELGGQRDLVQAMKRRVLELIQEKDRL 506
Cdd:COG1196  398 LAAQLEELEEAEEALLERLERLEEELEELEEAL 430

RUN_PLEKHM2

cd17680

RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...

14-161

1.18e-05

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

Pssm-ID: 439042 Cd Length: 145 Bit Score: 45.31 E-value: 1.18e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  14 LRAAVSAI--LQGY----GDGQGPVTDTSAELHRLCGCLELLLQFdqkeqkSFLGPRKDYWDFLCTALRRQRgnmepIHF 87
Cdd:cd17680    3 LRNISEAIksLQSYsssqEEEDVLITNENRELQRLCEALDHALLH------GLRRGNRGYWPFVKEFTHKET-----IKQ 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 282165733  88 VRSQDKLKTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFEL 161
Cdd:cd17680   72 IENLPNVTTDLGRGRAWLYLALNEGSLESYLRSFLENRKLVKKFYHKHALLRDSQRLELLLTLLSGLEFVQFDL 145

RUN_RUNDC3A

cd17699

RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ...

15-132

1.22e-05

RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN domain-containing protein 3A (RUNDC3A), also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. It contains a RUN domain.

Pssm-ID: 439061 Cd Length: 151 Bit Score: 45.40 E-value: 1.22e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  15 RAAVSAILQGYGdgQGPVTDTSAELHRLCGCLELLLQFDQKEQKSFLGP--RKDYWDFLCTALRRQRGNMepIHFVRSQD 92
Cdd:cd17699    7 RFSVKTLLEKYT--AEPIDDSSEEFVNFAAILEQILSHRFKGPVSWFSSdgQRGFWDYIRLACSKVPNNC--ISSIENME 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 282165733  93 KLKTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWY 132
Cdd:cd17699   83 NISTSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFY 122

RUN

smart00593

domain involved in Ras-like GTPase signaling;

101-163

1.25e-05

domain involved in Ras-like GTPase signaling;

Pssm-ID: 214736 [Multi-domain] Cd Length: 64 Bit Score: 42.99 E-value: 1.25e-05

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 282165733   101 GRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFELDL 163
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRDPEEGEQLLGLLVGLSALDFNLPV 63

COG4913

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

398-511

1.48e-05

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.48e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  398 TLVARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQ--------LSRCQEERAELQAQLEQKQQ 469
Cdd:COG4913   280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEERER 359

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 282165733  470 EAERRD---AMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQ 511
Cdd:COG4913   360 RRARLEallAALGLPLPASAEEFAALRAEAAALLEALEEELEALE 404

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

392-516

1.53e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 1.53e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   392 QVQTEVTLVARREEQAEvSLQDEIKSLRlglRKAEEQAQRQEQLLREQEGELQALRE-QLSRCQEERAELQAQLEQKQQE 470
Cdd:TIGR02168  380 QLETLRSKVAQLELQIA-SLNNEIERLE---ARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEE 455

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 282165733   471 AERRdamyQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSSM 516
Cdd:TIGR02168  456 LERL----EEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497

RUN_PLEKHM1

cd17679

RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...

11-163

1.68e-05

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

Pssm-ID: 439041 [Multi-domain] Cd Length: 171 Bit Score: 45.27 E-value: 1.68e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  11 TKDLRAAVSAILQGYGDGQGPVTDTSAELHRLCGCLE-LLLQ-----FDQKEQKSFLG-----PRKDYWDFLCTALRRQr 79
Cdd:cd17679    5 TKELSSSVKELQLEYVSSDEVVTSSDDGANTLCCVLEaIFLHglkdkFISKVSSVFSGdvdklPEPNFWPLLLKFSHRD- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  80 gnmepihfVRSQ-DKL---KTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALN 155
Cdd:cd17679   84 --------VIDQiEHLsqiTTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRDPEQLDILKSLLQGLE 155


                 ....*...
gi 282165733 156 GVAFELDL 163
Cdd:cd17679  156 SFQFELPY 163

Lebercilin

pfam15619

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...

410-511

1.89e-05

Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 45.66 E-value: 1.89e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  410 SLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQE--------ERAELQAQLEQKQQEAERRDAMYQE- 480
Cdd:pfam15619  64 RHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKlsedknlaEREELQKKLEQLEAKLEDKDEKIQDl 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 282165733  481 -------------ELGGQRDLVQAMKRRVLELIQEKDRLWQRLQ 511
Cdd:pfam15619 144 erklelenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187

Smc

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

401-511

1.91e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 1.91e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 401 ARREEQAEVSLQDEIKSLRlglRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAEL---QAQLEQKQQEAERRDAM 477
Cdd:COG1196  388 LLEALRAAAELAAQLEELE---EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALeeaAEEEAELEEEEEALLEL 464

                         90       100       110
                 ....*....|....*....|....*....|....
gi 282165733 478 YQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQ 511
Cdd:COG1196  465 LAELLEEAALLEAALAELLEELAEAAARLLLLLE 498

COG4913

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

392-509

2.01e-05

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.01e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  392 QVQTEVTLVARREEQAEVSLQ----DEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQK 467
Cdd:COG4913   313 RLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 282165733  468 QQEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQR 509
Cdd:COG4913   393 LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434

Smc

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

392-513

2.11e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 2.11e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 392 QVQTEVTLVARREEQAEVS-LQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQ---AQLEQK 467
Cdd:COG1196  224 ELEAELLLLKLRELEAELEeLEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLaelARLEQD 303

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 282165733 468 -------QQEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHL 513
Cdd:COG1196  304 iarleerRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

MAD

pfam05557

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...

401-516

2.14e-05

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

Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.43 E-value: 2.14e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  401 ARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQL----SRCQE---ERAELQAQL------EQK 467
Cdd:pfam05557  92 LNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLdllkAKASEaeqLRQNLEKQQsslaeaEQR 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 282165733  468 QQEAERRDAMYQEElggqRDLVQAMKRRVL---ELIQEKDRLWQRLQHLSSM 516
Cdd:pfam05557 172 IKELEFEIQSQEQD----SEIVKNSKSELAripELEKELERLREHNKHLNEN 219

hsdR

PRK11448

type I restriction enzyme EcoKI subunit R; Provisional

405-505

2.30e-05

type I restriction enzyme EcoKI subunit R; Provisional

Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 47.64 E-value: 2.30e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  405 EQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEELGG 484
Cdd:PRK11448  141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKE 220

                          90       100
                  ....*....|....*....|.
gi 282165733  485 QRDlvQAMKRrvLELIQEKDR 505
Cdd:PRK11448  221 ITD--QAAKR--LELSEEETR 237

CCDC158

pfam15921

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

392-498

2.43e-05

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

Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 2.43e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   392 QVQTEVTLVARR----EEQAEVSLQDEIKSLRLGLRKAEEqaqRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQK 467
Cdd:pfam15921  228 ELDTEISYLKGRifpvEDQLEALKSESQNKIELLLQQHQD---RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304

                           90       100       110
                   ....*....|....*....|....*....|.
gi 282165733   468 QQEAERRDAMYQEELGGQRDLVQAMKRRVLE 498
Cdd:pfam15921  305 QEQARNQNSMYMRQLSDLESTVSQLRSELRE 335

PRK00409

recombination and DNA strand exchange inhibitor protein; Reviewed

423-506

3.06e-05

recombination and DNA strand exchange inhibitor protein; Reviewed

Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 3.06e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 423 RKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEA-----ERRDAMYQEELGGQRDLVQAMKRRvl 497
Cdd:PRK00409 530 RELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAikeakKEADEIIKELRQLQKGGYASVKAH-- 607


                 ....*....
gi 282165733 498 ELIQEKDRL 506
Cdd:PRK00409 608 ELIEARKRL 616

mukB

PRK04863

chromosome partition protein MukB;

402-513

3.15e-05

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 3.15e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  402 RREEQAEVSLQDEIKSLRLGLRKAEEQaqrqEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAER-------- 473
Cdd:PRK04863  530 RQQQRAERLLAEFCKRLGKNLDDEDEL----EQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRlaarapaw 605

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 282165733  474 ---RDAMYQ------EELGGQRDLVQAMK---RRVLELIQEKDRLWQRLQHL 513
Cdd:PRK04863  606 laaQDALARlreqsgEEFEDSQDVTEYMQqllERERELTVERDELAARKQAL 657

MukB

COG3096

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...

401-515

3.41e-05

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

Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 3.41e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  401 ARREEQAEVSLQDEIKSLRLGLRKAEEQaqrqEQLLREQEGELQALREQLSRCQEERAELQAQLEQ-------------- 466
Cdd:COG3096   528 LRQQQNAERLLEEFCQRIGQQLDAAEEL----EELLAELEAQLEELEEQAAEAVEQRSELRQQLEQlrarikelaarapa 603

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 282165733  467 ---KQQEAERRDAMYQEELGGQRDLVQAMK---RRVLELIQEKDRLWQRLQHLSS 515
Cdd:COG3096   604 wlaAQDALERLREQSGEALADSQEVTAAMQqllEREREATVERDELAARKQALES 658

OmpH

pfam03938

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...

426-502

3.59e-05

Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 43.72 E-value: 3.59e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  426 EEQAQRQEQLLREQEGELQALREQL----SRCQEERAELQAQLEQKQQEAERRDAMYQEELGG-QRDLVQAMKRRVLELI 500
Cdd:pfam03938  25 EKKFKKRQAELEAKQKELQKLYEELqkdgALLEEEREEKEQELQKKEQELQQLQQKAQQELQKkQQELLQPIQDKINKAI 104


                  ..
gi 282165733  501 QE 502
Cdd:pfam03938 105 KE 106

MIC19_MIC25

pfam05300

MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ...

423-483

3.60e-05

MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ChChd6) are components of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. MIC19 plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology.

Pssm-ID: 461615 [Multi-domain] Cd Length: 173 Bit Score: 44.68 E-value: 3.60e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165733  423 RKAEEQAQRQEQLLREQEGELQALREQLSRC--------QEER---AELQAQLEQKQQEAERRDAMYQEELG 483
Cdd:pfam05300  74 RLEQEQAKVQEELARLAEREREAAQESLTRAilrerastEDERlkaQQLAKQLEEKEAELKKQDAFYKEQLA 145

COG4913

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

400-513

3.63e-05

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 3.63e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  400 VARREEQAE-----VSLQDEIKSLRLGLRKAEE-----QAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQ 469
Cdd:COG4913   244 LEDAREQIEllepiRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALRE 323

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 282165733  470 EAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHL 513
Cdd:COG4913   324 ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEAL 367

Smc

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

392-511

3.69e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 3.69e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 392 QVQTEVTLVARREEQAEVSLQDEIKSLRlglRKAEEQAQRQEQL------LREQEGELQALREQLSRCQEERAELQAQLE 465
Cdd:COG1196  299 RLEQDIARLEERRRELEERLEELEEELA---ELEEELEELEEELeeleeeLEEAEEELEEAEAELAEAEEALLEAEAELA 375

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 282165733 466 QKQQEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQ 511
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

403-515

3.75e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 3.75e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 403 REEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQ---QEAERRDAMYQ 479
Cdd:COG4372   21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNeqlQAAQAELAQAQ 100

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 282165733 480 EELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSS 515
Cdd:COG4372  101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEA 136

FYVE_PIKfyve_Fab1

cd15725

FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...

521-564

5.95e-05

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

Pssm-ID: 277264 [Multi-domain] Cd Length: 62 Bit Score: 41.16 E-value: 5.95e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 282165733 521 CVACSKIFGRFSRRYPCRLCGGLLCHACS--------MDYKKRDRCCPPCAQ 564
Cdd:cd15725   11 CYECSEKFTTFRRRHHCRLCGQIFCSRCCnqeipgkfIGYPGDLRVCTYCCK 62

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

392-502

6.63e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 6.63e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 392 QVQTEVTLVARREEQAEvSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEA 471
Cdd:COG4372   32 QLRKALFELDKLQEELE-QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110

                         90       100       110
                 ....*....|....*....|....*....|.
gi 282165733 472 ERRDAmYQEELGGQRDLVQAMKRRVLELIQE 502
Cdd:COG4372  111 EELQE-ELEELQKERQDLEQQRKQLEAQIAE 140

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

371-515

7.20e-05

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

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 7.20e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   371 LGEPWVLQGHATKEDSTVENPQVQTEVTLVARREEQAEVSLQdeikslrlglrKAEEQAQRQEQLLREQEGELQALREQL 450
Cdd:TIGR02169  284 LGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA-----------KLEAEIDKLLAEIEELEREIEEERKRR 352

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 282165733   451 SRCQEERAELQAQLEQKQQEAERRDAMYQE---ELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSS 515
Cdd:TIGR02169  353 DKLTEEYAELKEELEDLRAELEEVDKEFAEtrdELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

EmrA

COG1566

Multidrug resistance efflux pump EmrA [Defense mechanisms];

418-511

7.22e-05

Multidrug resistance efflux pump EmrA [Defense mechanisms];

Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.04 E-value: 7.22e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 418 LRLGLRKAEEQAQRQEQLLREQEGELQAlREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEELGGQRDLVQAmKRRVL 497
Cdd:COG1566   81 LQAALAQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEA-RAALD 158

                         90
                 ....*....|....
gi 282165733 498 ELIQEKDRLWQRLQ 511
Cdd:COG1566  159 AAQAQLEAAQAQLA 172

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

384-514

8.86e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 8.86e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   384 EDSTVENPQVQTEVTLVARREEQAE-VSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQA 462
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEElAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 282165733   463 QLEQKQQEAERRdamyQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLS 514
Cdd:TIGR02168  832 RIAATERRLEDL----EEQIEELSEDIESLAAEIEELEELIEELESELEALL 879

PRK02224

DNA double-strand break repair Rad50 ATPase;

383-506

9.05e-05

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 9.05e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 383 KEDSTVENPQVQTEVTLVARREEQAE--VSLQDEIKSLRlglrkaeEQAQRQEQLLREQEGELQALREQLSRCQEERAEL 460
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEdlVEAEDRIERLE-------ERREDLEELIAERRETIEEKRERAEELRERAAEL 549

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 282165733 461 QAQLEQKQQEAERRdamyQEELGGQRDLVQAMKRRVLELIQEKDRL 506
Cdd:PRK02224 550 EAEAEEKREAAAEA----EEEAEEAREEVAELNSKLAELKERIESL 591

Mitofilin

pfam09731

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...

406-503

9.81e-05

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.

Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 45.13 E-value: 9.81e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  406 QAEVSLQDEIKSLRLGLRK-AEEQAQRQE--------QLLREQEGELQALREQLsrcqeeRAELQAQLEQKQQEAERRda 476
Cdd:pfam09731 309 REEKHIERALEKQKEELDKlAEELSARLEevraadeaQLRLEFEREREEIRESY------EEKLRTELERQAEAHEEH-- 380

                          90       100
                  ....*....|....*....|....*..
gi 282165733  477 mYQEELGGQRdlvQAMKRRVLELIQEK 503
Cdd:pfam09731 381 -LKDVLVEQE---IELQREFLQDIKEK 403

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

399-495

1.02e-04

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.02e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 399 LVARREEQAEvSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQlsrcQEERAELQAQLEQKQQEAERRDAMY 478
Cdd:COG4942  144 LAPARREQAE-ELRADLAELAALRAELEAERAELEALLAELEEERAALEAL----KAERQKLLARLEKELAELAAELAEL 218

                         90
                 ....*....|....*..
gi 282165733 479 QEELGGQRDLVQAMKRR 495
Cdd:COG4942  219 QQEAEELEALIARLEAE 235

PRK12704

phosphodiesterase; Provisional

411-482

1.08e-04

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.08e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165733 411 LQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEEL 482
Cdd:PRK12704  73 FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL 144

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

403-513

1.17e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 1.17e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   403 REEQAEVS-LQDEIKSLRLGLRK-------AEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQE---A 471
Cdd:TIGR02168  806 DELRAELTlLNEEAANLRERLESlerriaaTERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasL 885

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 282165733   472 ERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHL 513
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927

PRK12704

phosphodiesterase; Provisional

401-519

1.23e-04

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.23e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 401 ARRE-----EQAEVSLQDEIKSLRlglRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRd 475
Cdd:PRK12704  47 AKKEaeaikKEALLEAKEEIHKLR---NEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK- 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 282165733 476 amyQEELggqrdlvQAMKRRVLELIQEKDrlwQRLQHLSSMAPE 519
Cdd:PRK12704 123 ---QQEL-------EKKEEELEELIEEQL---QELERISGLTAE 153

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

404-514

1.24e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 1.24e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   404 EEQAEVS-----LQDEIKSLRLGLRKAEEQAQRQEqlLREQEGELQALREQLSRCQEERAELQAQLEQ---KQQEAERRD 475
Cdd:TIGR02168  206 ERQAEKAerykeLKAELRELELALLVLRLEELREE--LEELQEELKEAEEELEELTAELQELEEKLEElrlEVSELEEEI 283

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 282165733   476 AMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLS 514
Cdd:TIGR02168  284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322

Myosin_tail_1

pfam01576

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

415-502

1.24e-04

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

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 1.24e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   415 IKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEElGGQRDLVQAMKR 494
Cdd:pfam01576  189 ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEE-TAQKNNALKKIR 267


                   ....*...
gi 282165733   495 RVLELIQE 502
Cdd:pfam01576  268 ELEAQISE 275

RUN_SNX29

cd17689

RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...

14-162

1.38e-04

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

Pssm-ID: 439051 Cd Length: 166 Bit Score: 42.60 E-value: 1.38e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  14 LRAAVSAILQGYGDGQGPVTDTSAELHRLCGCLELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPI--HFVRSQ 91
Cdd:cd17689    2 LLDAVKQCQIRFGGKTELATESDSRVSCLCAQLEAVLQHGLKTSRSPNLVSSAVTQVSGLAGSLGSAETEPTfwPFVKEH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  92 ---------DKLK---TPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAF 159
Cdd:cd17689   82 ltkhelerfELLKniwTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRDEERSSMLPNMAAGLGSILF 161


                 ...
gi 282165733 160 ELD 162
Cdd:cd17689  162 ALS 164

PRK12705

hypothetical protein; Provisional

402-519

1.38e-04

hypothetical protein; Provisional

Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 1.38e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 402 RREEQAEVSLQDEIKSLRLGLRKAeeQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEE 481
Cdd:PRK12705  30 RLAKEAERILQEAQKEAEEKLEAA--LLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQL 107

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 282165733 482 LGGQRdlvqAMKRRVLELIQEKDRLWQRLQHLSSMAPE 519
Cdd:PRK12705 108 EEREK----ALSARELELEELEKQLDNELYRVAGLTPE 141

CwlO1

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

406-482

1.62e-04

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 1.62e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 282165733 406 QAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEEL 482
Cdd:COG3883  129 DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205

GumC

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

387-480

1.65e-04

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.65e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 387 TVENPQVQTevtlvARRE-EQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSrcqeeraELQAQLE 465
Cdd:COG3206  287 TPNHPDVIA-----LRAQiAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELP-------ELEAELR 354

                         90
                 ....*....|....*
gi 282165733 466 QKQQEAERRDAMYQE 480
Cdd:COG3206  355 RLEREVEVARELYES 369

ClpA

COG0542

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...

394-485

1.96e-04

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

Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 1.96e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 394 QTEVTLVARREEQAEVS------LQDEIKSLRLGLRKAEEQAQRQEQLLREqegeLQALREQLSRCQEERAELQAQLEQK 467
Cdd:COG0542  422 QLEIEKEALKKEQDEASferlaeLRDELAELEEELEALKARWEAEKELIEE----IQELKEELEQRYGKIPELEKELAEL 497

                         90
                 ....*....|....*...
gi 282165733 468 QQEAERRDAMYQEELGGQ 485
Cdd:COG0542  498 EEELAELAPLLREEVTEE 515

YhaN

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

405-513

2.09e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.09e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 405 EQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQ--EGELQALREQLSRCQEERAELQaQLEQKQQEAERRDAMYQEEL 482
Cdd:COG4717  101 EEELEELEAELEELREELEKLEKLLQLLPLYQELEalEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEEL 179

                         90       100       110
                 ....*....|....*....|....*....|..
gi 282165733 483 GGQRDLV-QAMKRRVLELIQEKDRLWQRLQHL 513
Cdd:COG4717  180 EELLEQLsLATEEELQDLAEELEELQQRLAEL 211

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

411-514

2.15e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 2.15e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   411 LQDEIKSLRLGLRKAEEQAQRQEQL------------------LREQEGELQALREQLSRCQEERAELQAQLEQKQQEAE 472
Cdd:TIGR02168  191 LEDILNELERQLKSLERQAEKAERYkelkaelrelelallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLE 270

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 282165733   473 R-RDAMYQEElggqrDLVQAMKRRVLELIQEKDRLWQRLQHLS 514
Cdd:TIGR02168  271 ElRLEVSELE-----EEIEELQKELYALANEISRLEQQKQILR 308

OmpH

smart00935

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...

424-502

2.27e-04

Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 41.42 E-value: 2.27e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   424 KAEEQAQRQEQLLREQEGELQALREQLSR-----CQEERAELQAQLEQKQQEAERRDAMYQEEL-GGQRDLVQAMKRRVL 497
Cdd:smart00935  22 QLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlSEAAREKKEKELQKKVQEFQRKQQKLQQDLqKRQQEELQKILDKIN 101


                   ....*
gi 282165733   498 ELIQE 502
Cdd:smart00935 102 KAIKE 106

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

422-520

2.58e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 2.58e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   422 LRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEELGGQRDLVQAMKR---RVLE 498
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQlskELTE 758

                           90       100
                   ....*....|....*....|..
gi 282165733   499 LIQEKDRLWQRLQHLSSMAPEC 520
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEA 780

TPR_MLP1_2

pfam07926

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...

409-511

2.93e-04

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.

Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 41.09 E-value: 2.93e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  409 VSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEG---------------------ELQALREQLSRCQEERAELQAQ---- 463
Cdd:pfam07926   4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEiareaqqnyerelvlhaedikALQALREELNELKAEIAELKAEaesa 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 282165733  464 ---LEQKQQEAERRDAMYQEELggqrdlvQAMKRRVLELIQEKDRLWQRLQ 511
Cdd:pfam07926  84 kaeLEESEESWEEQKKELEKEL-------SELEKRIEDLNEQNKLLHDQLE 127

RUN_RUFY1

cd17694

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

46-155

3.07e-04

RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.

Pssm-ID: 439056 Cd Length: 156 Bit Score: 41.43 E-value: 3.07e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  46 LELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPIHFVRSQDKLKTPLGKGRAFIRFCLARGQLAEALQLCLLNS 125
Cdd:cd17694   41 LEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIATSARNLPELKTAVGRGRAWLHLALMQKKLADYLKVLIDRK 120

                         90       100       110
                 ....*....|....*....|....*....|
gi 282165733 126 ELTREWYGPRSpLLCPERQEDILDSLYALN 155
Cdd:cd17694  121 DLLSEFYEPGA-LMMEEEGAVIVGLLVGLN 149

Smc

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

392-511

3.14e-04

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 3.14e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 392 QVQTEVTLVARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEgELQALREQLSRCQEERAELQAQLEQKQQEA 471
Cdd:COG1196  408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-EEEALLELLAELLEEAALLEAALAELLEEL 486

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 282165733 472 ER---RDAMYQEELGGQRDLVQAMKRrvLELIQEKDRLWQRLQ 511
Cdd:COG1196  487 AEaaaRLLLLLEAEADYEGFLEGVKA--ALLLAGLRGLAGAVA 527

RUN1_DENND5A

cd17690

RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ...

49-159

3.48e-04

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

Pssm-ID: 439052 [Multi-domain] Cd Length: 209 Bit Score: 42.30 E-value: 3.48e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  49 LLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGN---MEPIHFVRSQD--------KLKTPLGKGRAFIRFCLARGQLAEA 117
Cdd:cd17690   80 LLHYQENRERKTTSSGLSTSGIILDSERRKSDAslaMPPLKISLIQDmrhiqnigEIKTDVGKARAWVRLSMEKKLLSRH 159

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 282165733 118 LQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAF 159
Cdd:cd17690  160 LKQLLSDHELTKKLYKRYAFLRCDDEKEQFLYHLLSFNAVDY 201

FYVE_scVPS27p_Vac1p_like

cd15736

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...

520-545

3.77e-04

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

Pssm-ID: 277275 [Multi-domain] Cd Length: 56 Bit Score: 38.70 E-value: 3.77e-04

                         10        20
                 ....*....|....*....|....*.
gi 282165733 520 CCVACSKIFGRFSRRYPCRLCGGLLC 545
Cdd:cd15736    1 CCHTCSRTFNLNIRAHHCRKCGKLFC 26

YhaN

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

427-516

4.61e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 4.61e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 427 EQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAmyQEELGGQRDLVQAMKRRVLELIQEKDRL 506
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK--LLQLLPLYQELEALEAELAELPERLEEL 151

                         90
                 ....*....|
gi 282165733 507 WQRLQHLSSM 516
Cdd:COG4717  152 EERLEELREL 161

YhaN

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

401-499

5.42e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 5.42e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 401 ARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLR-EQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAmyQ 479
Cdd:COG4717  151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE--E 228

                         90       100
                 ....*....|....*....|
gi 282165733 480 EELGGQRDLVQAMKRRVLEL 499
Cdd:COG4717  229 LEQLENELEAAALEERLKEA 248

COG4913

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

411-519

5.47e-04

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 5.47e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  411 LQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALR----------------EQLSRCQEERAELQA------QLEQKQ 468
Cdd:COG4913   615 LEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswdeidvasaeREIAELEAELERLDAssddlaALEEQL 694

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 282165733  469 QEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSSMAPE 519
Cdd:COG4913   695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

403-517

5.60e-04

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 5.60e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   403 REEQAEV-SLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDamyqEE 481
Cdd:TIGR02169  346 EEERKRRdKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS----EE 421

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 282165733   482 LGGQRDLVQAMKRRVLELIQEKD----RLWQRLQHLSSMA 517
Cdd:TIGR02169  422 LADLNAAIAGIEAKINELEEEKEdkalEIKKQEWKLEQLA 461

FYVE_Hrs

cd15720

FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...

519-562

5.72e-04

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: 38.14 E-value: 5.72e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 282165733 519 ECCVACSKIFGRFSRRYPCRLCGGLLCHACSMDY--------KKRDRCCPPC 562
Cdd:cd15720    6 DECHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSstipkfgiEKEVRVCDPC 57

DUF4670

pfam15709

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...

402-509

5.83e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.

Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.63 E-value: 5.83e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  402 RREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEE--RAELQAQLEQKQQEAERRDAMYQ 479
Cdd:pfam15709 373 KMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrRKLQELQRKKQQEEAERAEAEKQ 452

                          90       100       110
                  ....*....|....*....|....*....|
gi 282165733  480 EELGGQRDLVQAMKrRVLELIQEKDRLWQR 509
Cdd:pfam15709 453 RQKELEMQLAEEQK-RLMEMAEEERLEYQR 481

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

392-482

6.16e-04

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

Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 6.16e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 392 QVQTEVTLVARREEQ-AEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQE 470
Cdd:COG1579   67 EIEEVEARIKKYEEQlGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146

                         90
                 ....*....|..
gi 282165733 471 AERRDAMYQEEL 482
Cdd:COG1579  147 LDEELAELEAEL 158

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

394-512

6.16e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 6.16e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   394 QTEVTLVARREEQAEV---SLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQE 470
Cdd:TIGR02168  336 AEELAELEEKLEELKEeleSLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 282165733   471 AERRDamyQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQH 512
Cdd:TIGR02168  416 RERLQ---QEIEELLKKLEEAELKELQAELEELEEELEELQE 454

PRK09039

peptidoglycan -binding protein;

404-505

7.07e-04

peptidoglycan -binding protein;

Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 7.07e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 404 EEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLsrcqeerAELQAQLEQKQQEAERrdAMYQEELG 483
Cdd:PRK09039  72 ERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRA-------GELAQELDSEKQVSAR--ALAQVELL 142

                         90       100
                 ....*....|....*....|....*...
gi 282165733 484 GQRdlVQAMKRR------VLELIQEKDR 505
Cdd:PRK09039 143 NQQ--IAALRRQlaaleaALDASEKRDR 168

FYVE_ANFY1

cd15728

FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...

519-549

7.13e-04

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

Pssm-ID: 277267 [Multi-domain] Cd Length: 63 Bit Score: 38.17 E-value: 7.13e-04

                         10        20        30
                 ....*....|....*....|....*....|.
gi 282165733 519 ECCVACSKIFGRFSRRYPCRLCGGLLCHACS 549
Cdd:cd15728    8 DYCYECGVKFGITTRKHHCRHCGRLLCSKCS 38

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

390-505

7.19e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 7.19e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   390 NPQVQTEVTLVARREEQAEvSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQ 469
Cdd:TIGR02168  858 AAEIEELEELIEELESELE-ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 282165733   470 EAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDR 505
Cdd:TIGR02168  937 RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR 972

FYVE_RUFY1_like

cd15721

FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...

521-562

7.66e-04

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: 37.75 E-value: 7.66e-04

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 282165733 521 CVACSKIFGRFSRRYPCRLCGGLLCHACS------MDYKKRDRCCPPC 562
Cdd:cd15721   10 CQQCEKEFSLSRRKHHCRNCGGIFCNSCSdntmplPSSAKPVRVCDTC 57

DUF4659

pfam15558

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...

400-512

7.91e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.

Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.95 E-value: 7.91e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  400 VARREEQAEVSLQDEIKSLRLGLRKAEEQA----QRQEQLLREQEGELQALREQLSRCQEER---AELQAQLEQKQQEAE 472
Cdd:pfam15558  89 VIEKESRWREQAEDQENQRQEKLERARQEAeqrkQCQEQRLKEKEEELQALREQNSLQLQERleeACHKRQLKEREEQKK 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 282165733  473 RRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQH 512
Cdd:pfam15558 169 VQENNLSELLNHQARKVLVDCQAKAEELLRRLSLEQSLQR 208

CwlO1

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

410-491

8.21e-04

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 8.21e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 410 SLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERR-DAMYQEelGGQRDL 488
Cdd:COG3883   27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaRALYRS--GGSVSY 104


                 ...
gi 282165733 489 VQA 491
Cdd:COG3883  105 LDV 107

GumC

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

399-501

8.29e-04

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 8.29e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 399 LVARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQL----SRCQEERAELQAQLEQKQQEAERR 474
Cdd:COG3206  249 LGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIaalrAQLQQEAQRILASLEAELEALQAR 328

                         90       100
                 ....*....|....*....|....*..
gi 282165733 475 DAMYQEELGGQRDLVQAMKRRVLELIQ 501
Cdd:COG3206  329 EASLQAQLAQLEARLAELPELEAELRR 355

YhaN

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

392-502

8.34e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 8.34e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 392 QVQTEVTLVARREEqAEVSLQDEIKSLRLGLRKAEEQAQRQEqlLREQEGELQALREQLSRCQEERAELQAQLEQKQQEA 471
Cdd:COG4717  393 QAEEYQELKEELEE-LEEQLEELLGELEELLEALDEEELEEE--LEELEEELEELEEELEELREELAELEAELEQLEEDG 469

                         90       100       110
                 ....*....|....*....|....*....|.
gi 282165733 472 ERRDAMYQEELGGQRDLVQAMKRRVLELIQE 502
Cdd:COG4717  470 ELAELLQELEELKAELRELAEEWAALKLALE 500

FYVE_endofin

cd15729

FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...

515-564

9.17e-04

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

Pssm-ID: 277268 [Multi-domain] Cd Length: 68 Bit Score: 38.10 E-value: 9.17e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 282165733 515 SMAPECcVACSKIFGRFSRRYPCRLCGGLLCHACS--------MDYKKRdRCCPPCAQ 564
Cdd:cd15729   11 SEAPNC-MQCEVKFTFTKRRHHCRACGKVLCSACCslkarleyLDNKEA-RVCVPCYQ 66

YhaN

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

422-512

9.41e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 9.41e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 422 LRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAmYQEELGGQRDLVQAMKRrvLELIQ 501
Cdd:COG4717   76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAELPER--LEELE 152

                         90
                 ....*....|.
gi 282165733 502 EKDRLWQRLQH 512
Cdd:COG4717  153 ERLEELRELEE 163

CwlO1

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

405-476

1.05e-03

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.05e-03

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165733 405 EQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDA 476
Cdd:COG3883  146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217

PTZ00121

MAEBL; Provisional

401-498

1.06e-03

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.06e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  401 ARREEQAEVSLQDeikslrlgLRKAEEQAQRQEQLLREQEGELQAlREQLSRCQEERAELQAQLEQKQQEAERRDAMYQE 480
Cdd:PTZ00121 1612 AKKAEEAKIKAEE--------LKKAEEEKKKVEQLKKKEAEEKKK-AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682

                          90
                  ....*....|....*...
gi 282165733  481 ELGGQRDLVQAMKRRVLE 498
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEE 1700

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

392-476

1.13e-03

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.13e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 392 QVQTEVTLVARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEA 471
Cdd:COG4942  157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236


                 ....*
gi 282165733 472 ERRDA 476
Cdd:COG4942  237 AAAAE 241

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

415-518

1.18e-03

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 1.18e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 415 IKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEELGGQRDLVQAMKR 494
Cdd:COG4942  141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220

                         90       100
                 ....*....|....*....|....
gi 282165733 495 RVLELIQEKDRLWQRLQHLSSMAP 518
Cdd:COG4942  221 EAEELEALIARLEAEAAAAAERTP 244

CwlO1

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

410-494

1.28e-03

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.28e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 410 SLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRdamyQEELGgqrDLV 489
Cdd:COG3883   20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER----REELG---ERA 92


                 ....*
gi 282165733 490 QAMKR 494
Cdd:COG3883   93 RALYR 97

hsdR

PRK11448

type I restriction enzyme EcoKI subunit R; Provisional

384-519

1.38e-03

type I restriction enzyme EcoKI subunit R; Provisional

Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 1.38e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  384 EDSTVENPQVQTEV-TLVARREEQAEVSLQDEIKslrlgLRKAEEQAQRQEQLLREQEGELQALREQLsrcqeerAELQA 462
Cdd:PRK11448  138 EDPENLLHALQQEVlTLKQQLELQAREKAQSQAL-----AEAQQQELVALEGLAAELEEKQQELEAQL-------EQLQE 205

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 282165733  463 QLEQKQQEAERRDAMYQEELGGQRDLVQAMKRRvleLI--QEKDRLW----QRLQHLSSMAPE 519
Cdd:PRK11448  206 KAAETSQERKQKRKEITDQAAKRLELSEEETRI---LIdqQLRKAGWeadsKTLRFSKGARPE 265

GBP_C

cd16269

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...

406-503

1.43e-03

Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.02 E-value: 1.43e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 406 QAEVSLQDEIKSLRLgLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAE-LQAQLEQKQQEAERR-DAMYQEELG 483
Cdd:cd16269  188 QADQALTEKEKEIEA-ERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRqLKEKMEEERENLLKEqERALESKLK 266

                         90       100
                 ....*....|....*....|
gi 282165733 484 GQRDLVQAMKRRVLELIQEK 503
Cdd:cd16269  267 EQEALLEEGFKEQAELLQEE 286

COG5493

Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only] ...

402-482

1.44e-03

Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only];

Pssm-ID: 444244 [Multi-domain] Cd Length: 239 Bit Score: 40.35 E-value: 1.44e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 402 RREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQlEQKQQEAERRDAMYQEE 481
Cdd:COG5493   23 RYAVLGLLATKDGLEELLERLEKLEEQMRKWEEQLRKLEEEIKKLREQVRKLEEDVKRLEEQ-ERKLEEAMAEHSELREE 101


                 .
gi 282165733 482 L 482
Cdd:COG5493  102 L 102

PRK12704

phosphodiesterase; Provisional

402-481

1.45e-03

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 1.45e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 402 RREEQAEVSLQ-DEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQ----QEAERRDA 476
Cdd:PRK12704  70 RNEFEKELRERrNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIeeqlQELERISG 149


                 ....*
gi 282165733 477 MYQEE 481
Cdd:PRK12704 150 LTAEE 154

FYVE_scVPS27p_like

cd15760

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...

520-553

1.55e-03

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: 36.89 E-value: 1.55e-03

                         10        20        30
                 ....*....|....*....|....*....|....
gi 282165733 520 CCVACSKIFGRFSRRYPCRLCGGLLCHACSMDYK 553
Cdd:cd15760    7 RCDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRI 40

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

392-511

1.57e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 1.57e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 392 QVQTEVTLVARREEQAEVSL---QDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQ 468
Cdd:COG4372   42 KLQEELEQLREELEQAREELeqlEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 282165733 469 QEaerrdamyQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQ 511
Cdd:COG4372  122 KE--------RQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156

Golgin_A5

pfam09787

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...

383-515

1.58e-03

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

Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.90 E-value: 1.58e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  383 KEDSTVENPQVQTEVTLVA-----RREEQAE--VSLQDEIKSLRLGLRKAEEQAQRQEQLLREQegeLQALREQLSRCQE 455
Cdd:pfam09787  31 KEGSGVEGLDSSTALTLELeelrqERDLLREeiQKLRGQIQQLRTELQELEAQQQEEAESSREQ---LQELEEQLATERS 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282165733  456 ERAELQAQLEQKQQEAERrdamYQEELGGQRDLVQA-MKRRVLELIQEKDRLWQRLQHLSS 515
Cdd:pfam09787 108 ARREAEAELERLQEELRY----LEEELRRSKATLQSrIKDREAEIEKLRNQLTSKSQSSSS 164

GumC

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

394-510

1.59e-03

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 1.59e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 394 QTEVTLVARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQA-----QLEQKQ 468
Cdd:COG3206  193 EAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspviqQLRAQL 272

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 282165733 469 QEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRL 510
Cdd:COG3206  273 AELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

411-515

1.63e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 1.63e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 411 LQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLsrcQEERAELQAQLEQkQQEAERRDAMYQEELGGQRDLVQ 490
Cdd:COG4372   43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL---EELNEQLQAAQAE-LAQAQEELESLQEEAEELQEELE 118

                         90       100
                 ....*....|....*....|....*
gi 282165733 491 AMKRRVLELIQEKDRLWQRLQHLSS 515
Cdd:COG4372  119 ELQKERQDLEQQRKQLEAQIAELQS 143

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

377-519

1.78e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 1.78e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   377 LQGHATKEDSTVENPQVQTE------VTLVARREEQAE--VSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALRE 448
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAaterrlEDLEEQIEELSEdiESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282165733   449 QLsrcQEERAELQaQLEQKQQEAERrdamyqeELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSSMAPE 519
Cdd:TIGR02168  895 EL---EELSEELR-ELESKRSELRR-------ELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE 954

OmpH

smart00935

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...

411-474

2.12e-03

Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.72 E-value: 2.12e-03

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 282165733   411 LQDEIKSLRLGLRKAEEQAQRQEQLL-----REQEGELQALREQLsrcQEERAELQAQLEQKQQEAERR 474
Cdd:smart00935  30 RQAELEKLEKELQKLKEKLQKDAATLseaarEKKEKELQKKVQEF---QRKQQKLQQDLQKRQQEELQK 95

PTZ00491

major vault protein; Provisional

388-505

2.37e-03

major vault protein; Provisional

Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 40.77 E-value: 2.37e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 388 VENPQVQT-EVTLVARREE-QAEVSLQDEIKSlrlglrKAEEQAQRQEQLLREQE--GEL-------------------- 443
Cdd:PTZ00491 630 ITNVDVQSvEPVDERTRDSlQKSVQLAIEITT------KSQEAAARHQAELLEQEarGRLerqkmhdkakaeeqrtklle 703

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 282165733 444 ------------QALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEELGGQRdlvqamKRRVLELIQEKDR 505
Cdd:PTZ00491 704 lqaesaavessgQSRAEALAEAEARLIEAEAEVEQAELRAKALRIEAEAELEKLR------KRQELELEYEQAQ 771

FYVE_ZFYV1

cd15734

FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...

519-563

2.47e-03

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: 36.54 E-value: 2.47e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 282165733 519 ECCVaCSKIFGRFSRRYPCRLCGGLLCHACSMDYKKRD--------RCCPPCA 563
Cdd:cd15734   10 ECSV-CKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPsrgwdhpvRVCDPCA 61

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

392-514

2.61e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 2.61e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   392 QVQTEVTLVARREEQAEVSL------QDEIKSLRLGLRKAEEQAQRQEQLLREQ----EGELQALREQLSRCQEERAELQ 461
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALaelrkeLEELEEELEQLRKELEELSRQISALRKDlarlEAEVEQLEERIAQLSKELTELE 760

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 282165733   462 AQ---LEQKQQEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLS 514
Cdd:TIGR02168  761 AEieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816

ERM_helical

pfam20492

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...

401-474

2.68e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.

Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 37.98 E-value: 2.68e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 282165733  401 ARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERR 474
Cdd:pfam20492  22 TKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIARL 95

PRK02224

DNA double-strand break repair Rad50 ATPase;

400-514

2.88e-03

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 2.88e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 400 VARREEQAEVSLQD---EIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEqkqqEAERRDA 476
Cdd:PRK02224 326 LRDRLEECRVAAQAhneEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE----ELRERFG 401

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 282165733 477 MYQEELGGQRDLVQamkrrvlELIQEKDRLWQRLQHLS 514
Cdd:PRK02224 402 DAPVDLGNAEDFLE-------ELREERDELREREAELE 432

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

396-515

3.07e-03

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 3.07e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   396 EVTLVARREEQAEVS---LQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQL-EQKQQEA 471
Cdd:TIGR02169  771 EEDLHKLEEALNDLEarlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRiDLKEQIK 850

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 282165733   472 ERRDAmyQEELGGQrdlVQAMKRRVLELIQEKDRLWQRLQHLSS 515
Cdd:TIGR02169  851 SIEKE--IENLNGK---KEELEEELEELEAALRDLESRLGDLKK 889

FYVE_spVPS27p_like

cd15735

FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...

519-552

3.27e-03

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: 35.97 E-value: 3.27e-03

                         10        20        30
                 ....*....|....*....|....*....|....
gi 282165733 519 ECCVACSKIFGRFSRRYPCRLCGGLLCHACSMDY 552
Cdd:cd15735    7 DVCMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKS 40

DUF4686

pfam15742

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...

401-513

3.27e-03

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.

Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 40.05 E-value: 3.27e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  401 ARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGEL-QALREQLSRCQEERAELQaqleqkQQEAERRDAmyQ 479
Cdd:pfam15742 163 ASENEAKLKQQYQEEQQKRKLLDQNVNELQQQVRSLQDKEAQLeMTNSQQQLRIQQQEAQLK------QLENEKRKS--D 234

                          90       100       110
                  ....*....|....*....|....*....|....
gi 282165733  480 EELGGQRDLvqamKRRVLELIQEKDRLWQRLQHL 513
Cdd:pfam15742 235 EHLKSNQEL----SEKLSSLQQEKEALQEELQQV 264

RUN_RUBCN

cd17686

RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing ...

39-168

3.35e-03

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

Pssm-ID: 439048 Cd Length: 151 Bit Score: 38.40 E-value: 3.35e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  39 LHRLCGCLELLLQFDQKEQKSfLGPRKDYWDFLCTALRRQRGNMEPIHFVRSQDKLKTP-LGKGRAFIRFCLARGQLAEA 117
Cdd:cd17686   21 LQRLCRAVENILQHGLKEFQG-LNKEIDDWEFVQGLRWLQPTLAPSIEQQSRSSPSESEvSDKGRLWLRQSLQQHCLSSQ 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 282165733 118 LQLCLLNSELTREWYGPRSPLLCPERQEDILDSLyalngVAFELDlqQPDL 168
Cdd:cd17686  100 LQWLVSDKELLRKYYEDEAFLRQEGYATALLICL-----TAVELN--QPSL 143

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

383-506

3.55e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 3.55e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733   383 KEDSTVENPQVQTEVTLVARRE-EQAEVSLQDEIKSLRLGLRKAEEQAQ----RQEQLLREQEgELQALREQLSRCQEER 457
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSElEEEIEELQKELYALANEISRLEQQKQilreRLANLERQLE-ELEAQLEELESKLDEL 335

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 282165733   458 AELQAQLEQKQQEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRL 506
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

tolA

PRK09510

cell envelope integrity inner membrane protein TolA; Provisional

421-480

3.71e-03

cell envelope integrity inner membrane protein TolA; Provisional

Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.79 E-value: 3.71e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 282165733 421 GLRKAEEQAQRQEQ-----LLREQEGELQALREQlsrcqeERAELQAQLEQKQQEAERRDAMYQE 480
Cdd:PRK09510  73 SAKRAEEQRKKKEQqqaeeLQQKQAAEQERLKQL------EKERLAAQEQKKQAEEAAKQAALKQ 131

HAUS2

pfam15003

HAUS augmin-like complex subunit 2; This family of proteins is found in eukaryotes. Proteins ...

443-511

3.71e-03

HAUS augmin-like complex subunit 2; This family of proteins is found in eukaryotes. Proteins in this family are typically between 203 and 291 amino acids in length. HAUS augmin-like complex subunit 2 is alternatively called centrosomal protein of 27 kDa (CEP27). It localized in the microtubule organizing centre, the centrosome. These microtubules are part of the cytoskeleton and give the cell its shape, provides it with a platform for motility and are crucial for mitosis. This protein is part of the HAUS augmin-like complex. This interacts with the gamma-tubulin ring complex (gamma-TuRC) which is required for spindle generation. HAUS2 may also increase the tension between spindle and kinetochore allowing for chromosome segregation during mitosis. This protein is involved in mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis.

Pssm-ID: 373465 Cd Length: 191 Bit Score: 38.71 E-value: 3.71e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 282165733  443 LQALReQLSRCQEERAELQAQLEQKQQEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQ 511
Cdd:pfam15003  41 ISRLR-ELSNVQRELAQLNLELQGRKDDKDTADLTHVSEIEKKCEALQRMTTHLKAVIQNKDRIIARLQ 108

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

410-519

3.83e-03

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 3.83e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 410 SLQDEIKSLRLGLRKAEEQAQRQEQLLREQEgELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEELGGQRDLV 489
Cdd:COG4942  130 DFLDAVRRLQYLKYLAPARREQAEELRADLA-ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208

                         90       100       110
                 ....*....|....*....|....*....|
gi 282165733 490 QAMKRRVLELIQEKDRLWQRLQHLSSMAPE 519
Cdd:COG4942  209 AELAAELAELQQEAEELEALIARLEAEAAA 238

FYVE_CARP

cd15750

FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ...

521-562

3.95e-03

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

Pssm-ID: 277289 [Multi-domain] Cd Length: 47 Bit Score: 35.41 E-value: 3.95e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 282165733 521 CVACSKIFGRFSRRYPCRLCGGLLCHACSMDYKKRDRCCPPC 562
Cdd:cd15750    3 CESCGAKFSVFKRKRTCADCKRYFCSNCLSKEERGRRRCRRC 44

GumC

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

409-515

3.96e-03

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 3.96e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733 409 VSLQDEIKSLRLGLRKAEEQAQRQEQLLRE---------QEGELQALREQLSRCQEERAELQAQL--------------- 464
Cdd:COG3206  222 SELESQLAEARAELAEAEARLAALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYtpnhpdvialraqia 301

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 282165733 465 ---EQKQQEAERRDAMYQEElggqrdlVQAMKRRVLELIQEKDRLWQRLQHLSS 515
Cdd:COG3206  302 alrAQLQQEAQRILASLEAE-------LEALQAREASLQAQLAQLEARLAELPE 348

OmpH

pfam03938

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...

411-471

4.00e-03

Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 37.94 E-value: 4.00e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 282165733  411 LQDEIKSLRLGLRKAEEQAQRQEQLL----REQEGELQALREQLsrcQEERAELQAQLEQKQQEA 471
Cdd:pfam03938  31 RQAELEAKQKELQKLYEELQKDGALLeeerEEKEQELQKKEQEL---QQLQQKAQQELQKKQQEL 92

GAS

pfam13851

Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...

413-509

4.37e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.

Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 38.73 E-value: 4.37e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  413 DEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQ----KQ--QEAERRDAMYQEELGGQR 486
Cdd:pfam13851  26 ELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENyekdKQslKNLKARLKVLEKELKDLK 105

                          90       100
                  ....*....|....*....|...
gi 282165733  487 DLVQAMKRRVLELIQEKDRLWQR 509
Cdd:pfam13851 106 WEHEVLEQRFEKVERERDELYDK 128

ATP-synt_B

pfam00430

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...

412-496

4.93e-03

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006

Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 37.68 E-value: 4.93e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  412 QDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQL-SRCQEERAELQAQLEQkqqEAERRDAMYQEELGGQRDLVQ 490
Cdd:pfam00430  36 ADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAkKRAEKLKEEIVAAAEA---EAERIIEQAAAEIEQEKDRAL 112


                  ....*.
gi 282165733  491 AMKRRV 496
Cdd:pfam00430 113 AELRQQ 118

TPH

pfam13868

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

401-512

5.23e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 39.13 E-value: 5.23e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  401 ARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQegelQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQE 480
Cdd:pfam13868  87 QKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ----RQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLK 162

                          90       100       110
                  ....*....|....*....|....*....|..
gi 282165733  481 ELGGQRdlvQAMKRRVLELIQEKDRLWQRLQH 512
Cdd:pfam13868 163 EKAERE---EEREAEREEIEEEKEREIARLRA 191

DUF5401

pfam17380

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

423-498

5.67e-03

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

Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 39.72 E-value: 5.67e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165733  423 RKAEEQAQRQEQLLREQEG----ELQALREQ----LSRCQEERAELQAQLEQ-KQQEAER-RDAMYQEELGGQRDLVQAM 492
Cdd:pfam17380 413 RKIQQQKVEMEQIRAEQEEarqrEVRRLEEErareMERVRLEEQERQQQVERlRQQEEERkRKKLELEKEKRDRKRAEEQ 492


                  ....*.
gi 282165733  493 KRRVLE 498
Cdd:pfam17380 493 RRKILE 498

GumC